1kq3: Difference between revisions
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==CRYSTAL STRUCTURE OF A GLYCEROL DEHYDROGENASE (TM0423) FROM THERMOTOGA MARITIMA AT 1.5 A RESOLUTION== | ==CRYSTAL STRUCTURE OF A GLYCEROL DEHYDROGENASE (TM0423) FROM THERMOTOGA MARITIMA AT 1.5 A RESOLUTION== | ||
<StructureSection load='1kq3' size='340' side='right' caption='[[1kq3]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='1kq3' size='340' side='right' caption='[[1kq3]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1kq3]] is a 1 chain structure | <table><tr><td colspan='2'>[[1kq3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KQ3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jpu|1jpu]], [[1jq5|1jq5]], [[1jqa|1jqa]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jpu|1jpu]], [[1jq5|1jq5]], [[1jqa|1jqa]]</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=1kq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kq3 OCA], [http://pdbe.org/1kq3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kq3 RCSB], [http://www.ebi.ac.uk/pdbsum/1kq3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kq3 ProSAT], [http://www.topsan.org/Proteins/JCSG/1kq3 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=1kq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kq3 OCA], [http://pdbe.org/1kq3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kq3 RCSB], [http://www.ebi.ac.uk/pdbsum/1kq3 PDBsum], [http://www.topsan.org/Proteins/JCSG/1kq3 TOPSAN]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Miller, M D]] | [[Category: Miller, M D]] | ||
Revision as of 14:00, 1 February 2017
CRYSTAL STRUCTURE OF A GLYCEROL DEHYDROGENASE (TM0423) FROM THERMOTOGA MARITIMA AT 1.5 A RESOLUTIONCRYSTAL STRUCTURE OF A GLYCEROL DEHYDROGENASE (TM0423) FROM THERMOTOGA MARITIMA AT 1.5 A RESOLUTION
Structural highlights
Function[GLDA_THEMA] Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions (By similarity). 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 PubMedStructural genomics is emerging as a principal approach to define protein structure-function relationships. To apply this approach on a genomic scale, novel methods and technologies must be developed to determine large numbers of structures. We describe the design and implementation of a high-throughput structural genomics pipeline and its application to the proteome of the thermophilic bacterium Thermotoga maritima. By using this pipeline, we successfully cloned and attempted expression of 1,376 of the predicted 1,877 genes (73%) and have identified crystallization conditions for 432 proteins, comprising 23% of the T. maritima proteome. Representative structures from TM0423 glycerol dehydrogenase and TM0449 thymidylate synthase-complementing protein are presented as examples of final outputs from the pipeline. Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline.,Lesley SA, Kuhn P, Godzik A, Deacon AM, Mathews I, Kreusch A, Spraggon G, Klock HE, McMullan D, Shin T, Vincent J, Robb A, Brinen LS, Miller MD, McPhillips TM, Miller MA, Scheibe D, Canaves JM, Guda C, Jaroszewski L, Selby TL, Elsliger MA, Wooley J, Taylor SS, Hodgson KO, Wilson IA, Schultz PG, Stevens RC Proc Natl Acad Sci U S A. 2002 Sep 3;99(18):11664-9. Epub 2002 Aug 22. PMID:12193646[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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