2zjp: Difference between revisions
No edit summary |
No edit summary |
||
Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zjp]] is a 31 chain structure with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] and [http://en.wikipedia.org/wiki/Streptomyces_actuosus Streptomyces actuosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZJP FirstGlance]. <br> | <table><tr><td colspan='2'>[[2zjp]] is a 31 chain structure with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] and [http://en.wikipedia.org/wiki/Streptomyces_actuosus Streptomyces actuosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZJP FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO1:4-(HYDROXYMETHYL)-3-METHYL-1H-INDOLE-2-CARBOXYLIC+ACID'>NO1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO1:4-(HYDROXYMETHYL)-3-METHYL-1H-INDOLE-2-CARBOXYLIC+ACID'>NO1</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3GL:(2S,4S)-2-AMINO-4-HYDROXY-PENTANEDIOIC+ACID'>3GL</scene>, <scene name='pdbligand=BB9:(2Z)-2-AMINO-3-SULFANYLPROP-2-ENOIC+ACID'>BB9</scene>, <scene name='pdbligand=DBU:(2Z)-2-AMINOBUT-2-ENOIC+ACID'>DBU</scene>, <scene name='pdbligand=DHA:2-AMINO-ACRYLIC+ACID'>DHA</scene>, <scene name='pdbligand=MH6:3-HYDROXY-2-IMINOPROPANOIC+ACID'>MH6</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3GL:(2S,4S)-2-AMINO-4-HYDROXY-PENTANEDIOIC+ACID'>3GL</scene>, <scene name='pdbligand=BB9:(2Z)-2-AMINO-3-SULFANYLPROP-2-ENOIC+ACID'>BB9</scene>, <scene name='pdbligand=DBU:(2Z)-2-AMINOBUT-2-ENOIC+ACID'>DBU</scene>, <scene name='pdbligand=DHA:2-AMINO-ACRYLIC+ACID'>DHA</scene>, <scene name='pdbligand=MH6:3-HYDROXY-2-IMINOPROPANOIC+ACID'>MH6</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d8t|1d8t]], [[1e9w|1e9w]], [[1oln|1oln]], [[2c77|2c77]], [[2jq7|2jq7]], [[3cf5|3cf5]], [[2zjq|2zjq]], [[2zjr|2zjr]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d8t|1d8t]], [[1e9w|1e9w]], [[1oln|1oln]], [[2c77|2c77]], [[2jq7|2jq7]], [[3cf5|3cf5]], [[2zjq|2zjq]], [[2zjr|2zjr]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zjp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zjp RCSB], [http://www.ebi.ac.uk/pdbsum/2zjp PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zjp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zjp RCSB], [http://www.ebi.ac.uk/pdbsum/2zjp PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/RL11_DEIRA RL11_DEIRA]] This protein binds directly to 23S ribosomal RNA and also contacts the CTC protein (RL25).[HAMAP-Rule:MF_00736_B] [[http://www.uniprot.org/uniprot/RL22_DEIRA RL22_DEIRA]] This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).[HAMAP-Rule:MF_01331_B] The globular domain of the protein is located by the polypeptide exit tunnel on the outside of the subunit while an extended beta-hairpin forms part of the wall of the tunnel. Forms a pair of "tweezers" with L32 that hold together two different domains of the 23S rRNA. Interacts with the tunnel-blocking modified macrolide azithromycin. Upon binding of the macrolide troleadomycin to the ribosome, the tip of the beta-hairpin is displaced, which severely restricts the tunnel. This and experiments in E.coli have led to the suggestion that it is part of the gating mechanism involved in translation arrest in the absence of the protein export system.[HAMAP-Rule:MF_01331_B] [[http://www.uniprot.org/uniprot/RL3_DEIRA RL3_DEIRA]] One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit (By similarity).[HAMAP-Rule:MF_01325_B] [[http://www.uniprot.org/uniprot/RL34_DEIRA RL34_DEIRA]] Binds the 23S rRNA.[HAMAP-Rule:MF_00391] [[http://www.uniprot.org/uniprot/RL18_DEIRA RL18_DEIRA]] This is one of the proteins that binds and mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.[HAMAP-Rule:MF_01337_B] [[http://www.uniprot.org/uniprot/RL23_DEIRA RL23_DEIRA]] One of the early assembly protein (By similarity) it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Forms the main docking site for trigger factor binding to the ribosome (PubMed:16091460 and PubMed:16271892).[HAMAP-Rule:MF_01369] [[http://www.uniprot.org/uniprot/RL33_DEIRA RL33_DEIRA]] Binds the 23S rRNA and the E site tRNA.[HAMAP-Rule:MF_00294] [[http://www.uniprot.org/uniprot/RL19_DEIRA RL19_DEIRA]] This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site (By similarity). Binds the 23S rRNA.[HAMAP-Rule:MF_00402] [[http://www.uniprot.org/uniprot/RL32_DEIRA RL32_DEIRA]] Forms a cluster with L17 and L22, and with L22, a pair of "tweezers" that hold together all the domains of the 23S rRNA. Interacts with the antibiotic troleandomycin which blocks the peptide exit tunnel.[HAMAP-Rule:MF_00340] [[http://www.uniprot.org/uniprot/RL24_DEIRA RL24_DEIRA]] One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit (By similarity).[HAMAP-Rule:MF_01326_B] One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (TF) when it is bound to the ribosome; this contact may expose a hydrophobic crevice in TF (PubMed:16271892).[HAMAP-Rule:MF_01326_B] [[http://www.uniprot.org/uniprot/RL14_DEIRA RL14_DEIRA]] Forms part of two intersubunit bridges in the 70S ribosome (By similarity). Binds to 23S rRNA.[HAMAP-Rule:MF_01367] [[http://www.uniprot.org/uniprot/RL17_DEIRA RL17_DEIRA]] Binds to the 23S rRNA.[HAMAP-Rule:MF_01368] [[http://www.uniprot.org/uniprot/RL2_DEIRA RL2_DEIRA]] One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome (By similarity).[HAMAP-Rule:MF_01320_B] [[http://www.uniprot.org/uniprot/RL29_DEIRA RL29_DEIRA]] Binds the 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.[HAMAP-Rule:MF_00374] [[http://www.uniprot.org/uniprot/RL27_DEIRA RL27_DEIRA]] Binds the 5S and 23S rRNAs and also the tRNA in the P site.[HAMAP-Rule:MF_00539] [[http://www.uniprot.org/uniprot/RL30_DEIRA RL30_DEIRA]] Binds the 5S and 23S rRNAs.[HAMAP-Rule:MF_01371] [[http://www.uniprot.org/uniprot/RL35_DEIRA RL35_DEIRA]] Binds the 23S rRNA.[HAMAP-Rule:MF_00514] [[http://www.uniprot.org/uniprot/RL5_DEIRA RL5_DEIRA]] This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement (By similarity). Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.[HAMAP-Rule:MF_01333_B] [[http://www.uniprot.org/uniprot/RL13_DEIRA RL13_DEIRA]] This protein is one of the early assembly proteins of the 50S ribosomal subunit (By similarity). Binds to the 23S rRNA.[HAMAP-Rule:MF_01366_B] [[http://www.uniprot.org/uniprot/RL15_DEIRA RL15_DEIRA]] Binds to the 23S rRNA.[HAMAP-Rule:MF_01341_B] [[http://www.uniprot.org/uniprot/RL16_DEIRA RL16_DEIRA]] Binds the 5S and 23S rRNAs and is also seen to make contacts with the A and P site tRNAs. Interacts with A site tRNA mimics, and is probably one of the key factors, along with a helix of the 23S rRNA, in positioning tRNA stems in the peptidyl-transferase center.[HAMAP-Rule:MF_01342] [[http://www.uniprot.org/uniprot/RL21_DEIRA RL21_DEIRA]] Binds directly to 23S rRNA, probably serving to organize its structure.[HAMAP-Rule:MF_01363] [[http://www.uniprot.org/uniprot/RL4_DEIRA RL4_DEIRA]] One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly (By similarity).[HAMAP-Rule:MF_01328_B] Makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit.[HAMAP-Rule:MF_01328_B] This protein is located close to the polypeptide exit tunnel, and interacts with the modified macrolide azithromycin, which blocks the tunnel.[HAMAP-Rule:MF_01328_B] [[http://www.uniprot.org/uniprot/RL36_DEIRA RL36_DEIRA]] Binds the 23S rRNA.[HAMAP-Rule:MF_00251] [[http://www.uniprot.org/uniprot/RL25_DEIRA RL25_DEIRA]] This is one of 3 proteins that mediate the attachment of the 5S rRNA onto the large ribosomal subunit. This protein has three domains. The N-terminal one is bound on the solvent face, the middle domain fills the space between the 5S rRNA and the L11 arm contacting the 23S rRNA while the C-terminal domain is on the edge of the intersubunit interface and contacts the A site. The protein conformation changes upon binding of a tRNA mimic to the A site, although the mimic does not interact directly with CTC itself, consistent with CTCs presumed role in moderating A site binding.[HAMAP-Rule:MF_01334] [[http://www.uniprot.org/uniprot/RL6_DEIRA RL6_DEIRA]] It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center (By similarity). This protein binds to the 23S rRNA, and is important in its secondary structure.[HAMAP-Rule:MF_01365] [[http://www.uniprot.org/uniprot/RL20_DEIRA RL20_DEIRA]] Binds directly to 23S rRNA, probably serving to organize its structure.[HAMAP-Rule:MF_00382] [[http://www.uniprot.org/uniprot/NOSM_STRAS NOSM_STRAS]] Inhibits bacterial protein biosynthesis by binding to ribosomes. Specifically, binds to the complex of 23S rRNA and ribosomal protein L11 (RPLK) in the 50S ribosomal subunit. While allowing a weak binding of elongation factor G (EF-G) to the ribosome and subsequent GTP-hydrolysis, probably impairs conformational changes in both the ribosome and EF-G which are necessary for translocation. In vitro, inhibits Gram-positive bacteria S.aureus strain 209P (MIC=0.0009 ug/ml), S.aureus strain 133 (MIC=0.0019 ug/ml), S.aureus strain B3 (MIC=0.003 ug/ml), S.aureus strain Hb (MIC=0.003 ug/ml), M.citreus strain ATCC 8411 (MIC=0.0038 ug/ml), M.lysodeikticus strain ATCC 4698 (MIC=0.003 ug/ml), S.lutea strain ATCC 9341 (MIC=0.0011 ug/ml), S.faecalis strain ATCC 9790 (MIC=0.0007 ug/ml), S.viridans (MIC=0.0065 ug/ml), S.pyogenes hemolyticus strain Dig7 (MIC=0.00028 ug/ml), D.pneumoniae strain Til (MIC=0.00015 ug/ml), N.catrrhalis (MIC=0.0017 ug/ml), L.casei strain ATCC 6633 (MIC=0.003 ug/ml), B.cereus strain ATCC 6630 (MIC=0.0071 ug/ml) and various isolates of L.monocytogenes. In vitro, inhibits Gram-negative bacterium P.multocida strain A125 (MIC=0.0024 ug/ml) but not M.smegmatis strain ATCC 6630, S.typhimurium, A.aerogenes strain ATCC 8308, P.vulgaris, K.pneumoniae strain ATCC 10031, S.marcescens strain A476, P.aeruginosa strain Bass or B.bronchiseptica strain CN387. Does not inhibit Gram-negative bacterium E.coli strain ATCC 9637 but does inhibit purified ribosomes from E.coli. In vivo, has no systemic effect in mice infected with staphylococci or streptococci when applied orally or subcutaneously. Has a local effect in mice infected subcutaneously or intraperitoneally with staphylococci when applied immediately afterwards. Is not toxic to mice.<ref>PMID:7379912</ref> <ref>PMID:7038038</ref> <ref>PMID:12954336</ref> <ref>PMID:18380436</ref> <ref>PMID:20441189</ref> <ref>PMID:21836384</ref> <ref>PMID:893891</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 35: | Line 37: | ||
[[Category: Deinococcus radiodurans]] | [[Category: Deinococcus radiodurans]] | ||
[[Category: Streptomyces actuosus]] | [[Category: Streptomyces actuosus]] | ||
[[Category: Connell, S R | [[Category: Connell, S R]] | ||
[[Category: Fucini, P | [[Category: Fucini, P]] | ||
[[Category: Harms, J M | [[Category: Harms, J M]] | ||
[[Category: Schluenzen, F | [[Category: Schluenzen, F]] | ||
[[Category: Spahn, C M.T | [[Category: Spahn, C M.T]] | ||
[[Category: Stachelhaus, T | [[Category: Stachelhaus, T]] | ||
[[Category: Wilson, D N | [[Category: Wilson, D N]] | ||
[[Category: Zaborowska, Z | [[Category: Zaborowska, Z]] | ||
[[Category: Antibacterial]] | [[Category: Antibacterial]] | ||
[[Category: Antibiotic]] | [[Category: Antibiotic]] |