1wue

<StructureSection load='1wue' size='340' side='right'caption='[[1wue]], [[Resolution|resolution]] 2.10&Aring;' scene=''>

<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>

</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>

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== 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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1wue" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Entfa]]

[[Category: Almo, S C]]

[[Category: Burley, S K]]

[[Category: Fedorov, A A]]

[[Category: Fedorov, E V]]

[[Category: Gerlt, J A]]

[[Category: Structural genomic]]

[[Category: Yew, W S]]

[[Category: Unknown function]]