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<StructureSection load='1tm0' size='340' side='right'caption='[[1tm0]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='1tm0' size='340' side='right'caption='[[1tm0]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1tm0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brume Brume]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TM0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1tm0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_melitensis_bv._1_str._16M Brucella melitensis bv. 1 str. 16M]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TM0 FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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]] 2.8&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Proline_racemase Proline racemase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.4 5.1.1.4] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1tm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tm0 OCA], [https://pdbe.org/1tm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tm0 RCSB], [https://www.ebi.ac.uk/pdbsum/1tm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tm0 ProSAT], [https://www.topsan.org/Proteins/NESGC/1tm0 TOPSAN]</span></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=1tm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tm0 OCA], [https://pdbe.org/1tm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tm0 RCSB], [https://www.ebi.ac.uk/pdbsum/1tm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tm0 ProSAT], [https://www.topsan.org/Proteins/NESGC/1tm0 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/Y1586_BRUME Y1586_BRUME]] In vitro, catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp) and that of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp), albeit with very low efficiency. The physiological substrate may be different (PubMed:24980702). Displays neither proline racemase activity nor t3LHyp dehydratase activity (PubMed:17849014, PubMed:24980702).<ref>PMID:17849014</ref> <ref>PMID:24980702</ref> <ref>PMID:24980702</ref>
[https://www.uniprot.org/uniprot/Y1586_BRUME Y1586_BRUME] In vitro, catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp) and that of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp), albeit with very low efficiency. The physiological substrate may be different (PubMed:24980702). Displays neither proline racemase activity nor t3LHyp dehydratase activity (PubMed:17849014, PubMed:24980702).<ref>PMID:17849014</ref> <ref>PMID:24980702</ref> <ref>PMID:24980702</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=1tm0 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=1tm0 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Structural genomics efforts have produced structural information, either directly or by modeling, for thousands of proteins over the past few years. While many of these proteins have known functions, a large percentage of them have not been characterized at the functional level. The structural information has provided valuable functional insights on some of these proteins, through careful structural analyses, serendipity, and structure-guided functional screening. Some of the success stories based on structures solved at the Northeast Structural Genomics Consortium (NESG) are reported here. These include a novel methyl salicylate esterase with important role in plant innate immunity, a novel RNA methyltransferase (H. influenzae yggJ (HI0303)), a novel spermidine/spermine N-acetyltransferase (B. subtilis PaiA), a novel methyltransferase or AdoMet binding protein (A. fulgidus AF_0241), an ATP:cob(I)alamin adenosyltransferase (B. subtilis YvqK), a novel carboxysome pore (E. coli EutN), a proline racemase homolog with a disrupted active site (B. melitensis BME11586), an FMN-dependent enzyme (S. pneumoniae SP_1951), and a 12-stranded beta-barrel with a novel fold (V. parahaemolyticus VPA1032).
Functional insights from structural genomics.,Forouhar F, Kuzin A, Seetharaman J, Lee I, Zhou W, Abashidze M, Chen Y, Yong W, Janjua H, Fang Y, Wang D, Cunningham K, Xiao R, Acton TB, Pichersky E, Klessig DF, Porter CW, Montelione GT, Tong L J Struct Funct Genomics. 2007 Sep;8(2-3):37-44. Epub 2007 Jun 23. PMID:17588214<ref>PMID:17588214</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1tm0" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Brume]]
[[Category: Brucella melitensis bv. 1 str. 16M]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Proline racemase]]
[[Category: Acton TB]]
[[Category: Acton, T B]]
[[Category: Chen Y]]
[[Category: Chen, Y]]
[[Category: Cooper B]]
[[Category: Cooper, B]]
[[Category: Forouhar F]]
[[Category: Forouhar, F]]
[[Category: Ho CK]]
[[Category: Ho, C K]]
[[Category: Hunt JF]]
[[Category: Hunt, J F]]
[[Category: Ma L-C]]
[[Category: Ma, L C]]
[[Category: Montelione GT]]
[[Category: Montelione, G T]]
[[Category: Tong L]]
[[Category: Structural genomic]]
[[Category: Xiao R]]
[[Category: Tong, L]]
[[Category: Xiao, R]]
[[Category: Alpha-beta protein that resembles double-beta barrel]]
[[Category: In each of which an alpha helix is sandwiched]]
[[Category: Isomerase]]
[[Category: Nesg]]
[[Category: PSI, Protein structure initiative]]

Latest revision as of 08:42, 1 May 2024

Crystal Structure of the putative proline racemase from Brucella melitensis, Northeast Structural Genomics Target LR31

1tm0, resolution 2.80Å

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