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3h7v

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Revision as of 20:11, 5 August 2016

CRYSTAL STRUCTURE OF O-SUCCINYLBENZOATE SYNTHASE FROM THERMOSYNECHOCOCCUS ELONGATUS BP-1 complexed with MG in the active site

Structural highlights

3h7v is a 1 chain structure with sequence from Theeb. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	2ozt
Gene:	tlr1174 (THEEB)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[Q8DJP8_THEEB] Converts SHCHC to OSB (By similarity).[SAAS:SAAS001354_004_000967]

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 PubMed

The rate of protein evolution is determined by a combination of selective pressure on protein function and biophysical constraints on protein folding and structure. Determining the relative contributions of these properties is an unsolved problem in molecular evolution with broad implications for protein engineering and function prediction. As a case study, we examined the structural divergence of the rapidly evolving o-succinylbenzoate synthase (OSBS) family, which catalyzes a step in menaquinone synthesis in diverse microorganisms and plants. On average, the OSBS family is much more divergent than other protein families from the same set of species, with the most divergent family members sharing <15% sequence identity. Comparing 11 representative structures revealed that loss of quaternary structure and large deletions or insertions are associated with the family's rapid evolution. Neither of these properties has been investigated in previous studies to identify factors that affect the rate of protein evolution. Intriguingly, one subfamily retained a multimeric quaternary structure and has small insertions and deletions compared with related enzymes that catalyze diverse reactions. Many proteins in this subfamily catalyze both OSBS and N-succinylamino acid racemization (NSAR). Retention of ancestral structural characteristics in the NSAR/OSBS subfamily suggests that the rate of protein evolution is not proportional to the capacity to evolve new protein functions. Instead, structural features that are conserved among proteins with diverse functions might contribute to the evolution of new functions.

Loss of quaternary structure is associated with rapid sequence divergence in the OSBS family.,Odokonyero D, Sakai A, Patskovsky Y, Malashkevich VN, Fedorov AA, Bonanno JB, Fedorov EV, Toro R, Agarwal R, Wang C, Ozerova ND, Yew WS, Sauder JM, Swaminathan S, Burley SK, Almo SC, Glasner ME Proc Natl Acad Sci U S A. 2014 May 28. pii: 201318703. PMID:24872444^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Odokonyero D, Sakai A, Patskovsky Y, Malashkevich VN, Fedorov AA, Bonanno JB, Fedorov EV, Toro R, Agarwal R, Wang C, Ozerova ND, Yew WS, Sauder JM, Swaminathan S, Burley SK, Almo SC, Glasner ME. Loss of quaternary structure is associated with rapid sequence divergence in the OSBS family. Proc Natl Acad Sci U S A. 2014 May 28. pii: 201318703. PMID:24872444 doi:http://dx.doi.org/10.1073/pnas.1318703111

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3h7v"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF O-SUCCINYLBENZOATE SYNTHASE FROM THERMOSYNECHOCOCCUS ELONGATUS BP-1 complexed with MG in the active site==
 <StructureSection load='3h7v' size='340' side='right' caption='[[3h7v]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ozt|2ozt]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tlr1174 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197221 THEEB])</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=3h7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h7v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h7v RCSB], [http://www.ebi.ac.uk/pdbsum/3h7v 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=3h7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h7v OCA], [http://pdbe.org/3h7v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3h7v RCSB], [http://www.ebi.ac.uk/pdbsum/3h7v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3h7v ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 20: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=3h7v ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 30: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3h7v" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

3h7v

From Proteopedia

Revision as of 20:11, 5 August 2016

CRYSTAL STRUCTURE OF O-SUCCINYLBENZOATE SYNTHASE FROM THERMOSYNECHOCOCCUS ELONGATUS BP-1 complexed with MG in the active site

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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