View source for 1vq4


==The structure of the transition state analogue "DAA" bound to the large ribosomal subunit of Haloarcula marismortui==
<StructureSection load='1vq4' size='340' side='right'caption='[[1vq4]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1vq4]] is a 31 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloarcula_marismortui Haloarcula marismortui]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VQ4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=1MA:6-HYDRO-1-METHYLADENOSINE-5-MONOPHOSPHATE'>1MA</scene>, <scene name='pdbligand=2OP:(2S)-2-HYDROXYPROPANOIC+ACID'>2OP</scene>, <scene name='pdbligand=5AA:N6-DIMETHYL-3-AMINO-ADENOSINE-5-MONOPHOSPHATE'>5AA</scene>, <scene name='pdbligand=OMG:O2-METHYLGUANOSINE-5-MONOPHOSPHATE'>OMG</scene>, <scene name='pdbligand=OMU:O2-METHYLURIDINE+5-MONOPHOSPHATE'>OMU</scene>, <scene name='pdbligand=PO2:HYPOPHOSPHITE'>PO2</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5-MONOPHOSPHATE'>PSU</scene>, <scene name='pdbligand=UR3:3-METHYLURIDINE-5-MONOPHOSHATE'>UR3</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1s72|1s72]], [[1jj2|1jj2]], [[1kqs|1kqs]], [[1m90|1m90]], [[1q7y|1q7y]], [[1q81|1q81]], [[1q82|1q82]], [[1q86|1q86]], [[1qvf|1qvf]], [[1qvg|1qvg]], [[1ffk|1ffk]], [[1ffz|1ffz]], [[1fgo|1fgo]], [[1vq5|1vq5]], [[1vq6|1vq6]], [[1vq7|1vq7]], [[1vq8|1vq8]], [[1vq9|1vq9]], [[1vqk|1vqk]], [[1vql|1vql]], [[1vqm|1vqm]], [[1vqn|1vqn]], [[1vqo|1vqo]], [[1vqp|1vqp]]</div></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vq4 OCA], [https://pdbe.org/1vq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vq4 RCSB], [https://www.ebi.ac.uk/pdbsum/1vq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vq4 ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/RL23_HALMA RL23_HALMA]] Binds to a specific region on the 23S rRNA. Located at the polypeptide exit tunnel on the outside of the subunit.[HAMAP-Rule:MF_01369] [[https://www.uniprot.org/uniprot/RL5_HALMA RL5_HALMA]] This is 1 of 5 proteins that mediates the attachment of the 5S rRNA onto the large ribosomal subunit, stabilizing the orientation of adjacent RNA domains. Forms part of the central protuberance. Modeling places the A and P site tRNAs in close proximity to this protein; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. In the 70S ribosome it is thought to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement.[HAMAP-Rule:MF_01333_A] [[https://www.uniprot.org/uniprot/RL31_HALMA RL31_HALMA]] Binds to the 23S rRNA. Located at the polypeptide exit tunnel on the outside of the subunit.[HAMAP-Rule:MF_00410] [[https://www.uniprot.org/uniprot/RL18E_HALMA RL18E_HALMA]] Stabilizes the tertiary rRNA structure within the 23S rRNA domain (domain II) to which it binds.[HAMAP-Rule:MF_00329] [[https://www.uniprot.org/uniprot/RL24_HALMA RL24_HALMA]] 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_A]  Stabilizes the tertiary rRNA structure within the 23S rRNA domain (domain I) to which it binds. Located at the polypeptide exit tunnel on the outside of the subunit.[HAMAP-Rule:MF_01326_A] [[https://www.uniprot.org/uniprot/RL19E_HALMA RL19E_HALMA]] Binds to the 23S rRNA. Located at the polypeptide exit tunnel on the outside of the subunit.[HAMAP-Rule:MF_01475] [[https://www.uniprot.org/uniprot/RL39_HALMA RL39_HALMA]] Binds to the 23S rRNA. Forms part of the polypeptide exit tunnel.[HAMAP-Rule:MF_00629] [[https://www.uniprot.org/uniprot/RL24E_HALMA RL24E_HALMA]] Binds to the 23S rRNA.[HAMAP-Rule:MF_00773] [[https://www.uniprot.org/uniprot/RL14_HALMA RL14_HALMA]] Forms part of two intersubunit bridges in the 70S ribosome (By similarity). Binds to 23S rRNA.[HAMAP-Rule:MF_01367] [[https://www.uniprot.org/uniprot/RL18_HALMA RL18_HALMA]] This is one of 5 proteins that mediate the attachment of the 5S rRNA onto the large ribosomal subunit, where it forms part of the central protuberance and stabilizes the orientation of adjacent RNA domains.[HAMAP-Rule:MF_01337_A] [[https://www.uniprot.org/uniprot/RL37_HALMA RL37_HALMA]] Binds to the 23S rRNA.[HAMAP-Rule:MF_00547] [[https://www.uniprot.org/uniprot/RL4_HALMA RL4_HALMA]] 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_A]  Makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit.[HAMAP-Rule:MF_01328_A]  Forms part of the polypeptide exit tunnel, in which it helps forms a bend with protein L22. Contacts the macrolide antibiotic spiramycin in the polypeptide exit tunnel.[HAMAP-Rule:MF_01328_A] [[https://www.uniprot.org/uniprot/RL32_HALMA RL32_HALMA]] Binds to the 23S rRNA.[HAMAP-Rule:MF_00810] [[https://www.uniprot.org/uniprot/RL30_HALMA RL30_HALMA]] This is one of 5 proteins that mediate the attachment of the 5S rRNA onto the large ribosomal subunit, stabilizing the orientation of adjacent RNA domains.[HAMAP-Rule:MF_01371] [[https://www.uniprot.org/uniprot/RL7A_HALMA RL7A_HALMA]] Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, box H/ACA and box C/D sRNAs (By similarity).[HAMAP-Rule:MF_00326] [[https://www.uniprot.org/uniprot/RL13_HALMA RL13_HALMA]] This protein is one of the early assembly proteins of the 50S ribosomal subunit (By similarity). Binds to 23S rRNA.[HAMAP-Rule:MF_01366] [[https://www.uniprot.org/uniprot/RL15_HALMA RL15_HALMA]] Binds to the 23S rRNA.[HAMAP-Rule:MF_01341_A] [[https://www.uniprot.org/uniprot/RL22_HALMA RL22_HALMA]] This protein binds specifically to 23S rRNA. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).[HAMAP-Rule:MF_01331]  Contacts all 6 domains of the 23S rRNA, helping stabilize their relative orientation. An extended beta-hairpin in the C-terminus forms part of the polypeptide exit tunnel, in which it helps forms a bend with protein L4, while most of the rest of the protein is located at the polypeptide exit tunnel on the outside of the subunit.[HAMAP-Rule:MF_01331] [[https://www.uniprot.org/uniprot/RL6_HALMA RL6_HALMA]] This protein binds to the 23S rRNA, and is important in its secondary structure. 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.[HAMAP-Rule:MF_01365] [[https://www.uniprot.org/uniprot/RL2_HALMA RL2_HALMA]] 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_A] [[https://www.uniprot.org/uniprot/RL29_HALMA RL29_HALMA]] Stabilizes the tertiary rRNA structure within the 23S rRNA domain (domain I) to which it binds. Located at the polypeptide exit tunnel on the outside of the subunit.[HAMAP-Rule:MF_00374] [[https://www.uniprot.org/uniprot/RLA0_HALMA RLA0_HALMA]] Ribosomal protein L10e is the functional equivalent of E.coli protein L10.[HAMAP-Rule:MF_00280] [[https://www.uniprot.org/uniprot/RL21_HALMA RL21_HALMA]] This is one of 5 proteins that mediate the attachment of the 5S rRNA onto the large ribosomal subunit, stabilizing the orientation of adjacent RNA domains.[HAMAP-Rule:MF_00369] [[https://www.uniprot.org/uniprot/RL44E_HALMA RL44E_HALMA]] Binds to the 23S rRNA. Binds deacetylated tRNA in the E site; when the tRNA binds a stretch of 7 amino acids are displaced to allow binding.[HAMAP-Rule:MF_01476] 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vq/1vq4_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1vq4 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peptide bond formation is catalyzed at the peptidyl transferase center (PTC) of the large ribosomal subunit. Crystal structures of the large ribosomal subunit of Haloarcula marismortui (Hma) complexed with several analogs that represent either the substrates or the transition state intermediate of the peptidyl transferase reaction show that this reaction proceeds through a tetrahedral intermediate with S chirality. The oxyanion of the tetrahedral intermediate interacts with a water molecule that is positioned by nucleotides A2637 (E. coli numbering, 2602) and (methyl)U2619(2584). There are no Mg2+ ions or monovalent metal ions observed in the PTC that could directly promote catalysis. The A76 2' hydroxyl of the peptidyl-tRNA is hydrogen bonded to the alpha-amino group and could facilitate peptide bond formation by substrate positioning and by acting as a proton shuttle between the alpha-amino group and the A76 3' hydroxyl of the peptidyl-tRNA.

Structural insights into the roles of water and the 2' hydroxyl of the P site tRNA in the peptidyl transferase reaction.,Schmeing TM, Huang KS, Kitchen DE, Strobel SA, Steitz TA Mol Cell. 2005 Nov 11;20(3):437-48. PMID:16285925<ref>PMID:16285925</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1vq4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ribosome 3D structures|Ribosome 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Haloarcula marismortui]]
[[Category: Large Structures]]
[[Category: Schmeing, T M]]
[[Category: Steitz, T A]]
[[Category: Peptidyl transferase reaction]]
[[Category: Protein-protein complex]]
[[Category: Protein-rna complex]]
[[Category: Ribosome]]
[[Category: Ribosome 50]]
[[Category: Rna-rna complex]]