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==Crystal structure of protein GI:29375081, unknown member of enolase superfamily from enterococcus faecalis V583==
==Crystal structure of protein GI:29375081, unknown member of enolase superfamily from enterococcus faecalis V583==
<StructureSection load='1wue' size='340' side='right' caption='[[1wue]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1wue' size='340' side='right'caption='[[1wue]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1wue]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Entfa Entfa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WUE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WUE FirstGlance]. <br>
<table><tr><td colspan='2'>[[1wue]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis_V583 Enterococcus faecalis V583]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WUE FirstGlance]. <br>
</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=1wue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wue OCA], [http://pdbe.org/1wue PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wue RCSB], [http://www.ebi.ac.uk/pdbsum/1wue PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wue ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1wue TOPSAN]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</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=1wue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wue OCA], [https://pdbe.org/1wue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wue RCSB], [https://www.ebi.ac.uk/pdbsum/1wue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wue ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1wue TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MENC_ENTFA MENC_ENTFA] Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB) (PubMed:24872444). Also acts as a N-succinylamino acid racemase (NSAR) that catalyzes the racemization of N-succinyl-L-phenylglycine (PubMed:24872444). Since the gene is encoded in a menaquinone synthesis operon, OSB synthase is probably the physiological activity. A pathway that requires NSAR activity has not been identified in this species, so whether NSAR is also a biological activity is unknown (PubMed:24872444).<ref>PMID:24872444</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1wue 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=1wue ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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 &lt;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<ref>PMID:24872444</ref>
==See Also==
 
*[[Mandelate racemase/muconate lactonizing enzyme 3D structures|Mandelate racemase/muconate lactonizing enzyme 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1wue" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Entfa]]
[[Category: Enterococcus faecalis V583]]
[[Category: Almo, S C]]
[[Category: Large Structures]]
[[Category: Burley, S K]]
[[Category: Almo SC]]
[[Category: Fedorov, A A]]
[[Category: Burley SK]]
[[Category: Fedorov, E V]]
[[Category: Fedorov AA]]
[[Category: Gerlt, J A]]
[[Category: Fedorov EV]]
[[Category: Structural genomic]]
[[Category: Gerlt JA]]
[[Category: Yew, W S]]
[[Category: Yew WS]]
[[Category: Enolase superfamily]]
[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
[[Category: PSI, Protein structure initiative]]
[[Category: Unknown function]]

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