1tm0

From Proteopedia

(Difference between revisions)

Revision as of 10:26, 10 September 2015

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

Structural highlights

1tm0 is a 2 chain structure with sequence from Brume. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Activity:	Proline racemase, with EC number 5.1.1.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, TOPSAN

Function

[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).^[1] ^[2] ^[3]

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

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^[4]

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

References

↑ Goytia M, Chamond N, Cosson A, Coatnoan N, Hermant D, Berneman A, Minoprio P. Molecular and structural discrimination of proline racemase and hydroxyproline-2-epimerase from nosocomial and bacterial pathogens. PLoS One. 2007 Sep 12;2(9):e885. PMID:17849014 doi:http://dx.doi.org/10.1371/journal.pone.0000885
↑ Zhao S, Sakai A, Zhang X, Vetting MW, Kumar R, Hillerich B, San Francisco B, Solbiati J, Steves A, Brown S, Akiva E, Barber A, Seidel RD, Babbitt PC, Almo SC, Gerlt JA, Jacobson MP. Prediction and characterization of enzymatic activities guided by sequence similarity and genome neighborhood networks. Elife. 2014 Jun 30;3. doi: 10.7554/eLife.03275. PMID:24980702 doi:http://dx.doi.org/10.7554/eLife.03275
↑ Zhao S, Sakai A, Zhang X, Vetting MW, Kumar R, Hillerich B, San Francisco B, Solbiati J, Steves A, Brown S, Akiva E, Barber A, Seidel RD, Babbitt PC, Almo SC, Gerlt JA, Jacobson MP. Prediction and characterization of enzymatic activities guided by sequence similarity and genome neighborhood networks. Elife. 2014 Jun 30;3. doi: 10.7554/eLife.03275. PMID:24980702 doi:http://dx.doi.org/10.7554/eLife.03275
↑ 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. Functional insights from structural genomics. J Struct Funct Genomics. 2007 Sep;8(2-3):37-44. Epub 2007 Jun 23. PMID:17588214 doi:10.1007/s10969-007-9018-3

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/1tm0"

@@ Line 2: / Line 2: @@
 <StructureSection load='1tm0' size='340' side='right' caption='[[1tm0]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1tm0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Brucella_melitensis Brucella melitensis]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TM0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1tm0]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proline_racemase Proline racemase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.4 5.1.1.4] </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=1tm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tm0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tm0 RCSB], [http://www.ebi.ac.uk/pdbsum/1tm0 PDBsum], [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tm0 OCA], [http://pdbe.org/1tm0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tm0 RCSB], [http://www.ebi.ac.uk/pdbsum/1tm0 PDBsum], [http://www.topsan.org/Proteins/NESGC/1tm0 TOPSAN]</span></td></tr>
 </table>
+== Function ==
+[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 27: @@
 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/>
 __TOC__
 </StructureSection>
-[[Category: Brucella melitensis]]
+[[Category: Brume]]
 [[Category: Proline racemase]]
 [[Category: Acton, T B]]

1tm0

From Proteopedia

Revision as of 10:26, 10 September 2015

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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