3lpe: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3lpe]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LPE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LPE FirstGlance]. <br> | <table><tr><td colspan='2'>[[3lpe]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LPE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LPE FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ewg|3ewg]], [[1ryq|1ryq]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ewg|3ewg]], [[1ryq|1ryq]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MJ0372 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii]), rpoE2, MJ0396 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MJ0372 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii]), rpoE2, MJ0396 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] </span></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=3lpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lpe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lpe RCSB], [http://www.ebi.ac.uk/pdbsum/3lpe 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=3lpe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lpe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lpe RCSB], [http://www.ebi.ac.uk/pdbsum/3lpe PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/NUSG_METJA NUSG_METJA]] Stimulates transcription elongation.<ref>PMID:20197319</ref> [[http://www.uniprot.org/uniprot/RPOE2_METJA RPOE2_METJA]] Stimulates transcription elongation.<ref>PMID:20197319</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: DNA-directed RNA polymerase]] | [[Category: DNA-directed RNA polymerase]] | ||
[[Category: Methanocaldococcus jannaschii]] | [[Category: Methanocaldococcus jannaschii]] | ||
[[Category: Cheung, A C.M | [[Category: Cheung, A C.M]] | ||
[[Category: Cramer, P | [[Category: Cramer, P]] | ||
[[Category: Damsma, G E | [[Category: Damsma, G E]] | ||
[[Category: Grohmann, D | [[Category: Grohmann, D]] | ||
[[Category: Hirtreiter, A | [[Category: Hirtreiter, A]] | ||
[[Category: Klose, D | [[Category: Klose, D]] | ||
[[Category: Martin, A C.R | [[Category: Martin, A C.R]] | ||
[[Category: Vojnic, E | [[Category: Vojnic, E]] | ||
[[Category: Werner, F | [[Category: Werner, F]] | ||
[[Category: Archaea]] | [[Category: Archaea]] | ||
[[Category: Dna-directed rna polymerase]] | [[Category: Dna-directed rna polymerase]] |
Revision as of 00:55, 25 December 2014
Crystal structure of Spt4/5NGN heterodimer complex from Methanococcus jannaschiiCrystal structure of Spt4/5NGN heterodimer complex from Methanococcus jannaschii
Structural highlights
Function[NUSG_METJA] Stimulates transcription elongation.[1] [RPOE2_METJA] Stimulates transcription elongation.[2] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSpt5 is the only known RNA polymerase-associated factor that is conserved in all three domains of life. We have solved the structure of the Methanococcus jannaschii Spt4/5 complex by X-ray crystallography, and characterized its function and interaction with the archaeal RNAP in a wholly recombinant in vitro transcription system. Archaeal Spt4 and Spt5 form a stable complex that associates with RNAP independently of the DNA-RNA scaffold of the elongation complex. The association of Spt4/5 with RNAP results in a stimulation of transcription processivity, both in the absence and the presence of the non-template strand. A domain deletion analysis reveals the molecular anatomy of Spt4/5--the Spt5 Nus-G N-terminal (NGN) domain is the effector domain of the complex that both mediates the interaction with RNAP and is essential for its elongation activity. Using a mutagenesis approach, we have identified a hydrophobic pocket on the Spt5 NGN domain as binding site for RNAP, and reciprocally the RNAP clamp coiled-coil motif as binding site for Spt4/5. Spt4/5 stimulates transcription elongation through the RNA polymerase clamp coiled-coil motif.,Hirtreiter A, Damsma GE, Cheung AC, Klose D, Grohmann D, Vojnic E, Martin AC, Cramer P, Werner F Nucleic Acids Res. 2010 Jul 1;38(12):4040-51. Epub 2010 Mar 2. PMID:20197319[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- DNA-directed RNA polymerase
- Methanocaldococcus jannaschii
- Cheung, A C.M
- Cramer, P
- Damsma, G E
- Grohmann, D
- Hirtreiter, A
- Klose, D
- Martin, A C.R
- Vojnic, E
- Werner, F
- Archaea
- Dna-directed rna polymerase
- Evolution
- Metal-binding
- Nucleotidyltransferase
- Nusg
- Spt4
- Spt5
- Transcription
- Transcription regulation
- Transferase
- Zinc-finger