3vfl: Difference between revisions
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==Structure, Function, Stability and Knockout Phenotype of Dihydrodipicolinate Synthase from Streptococcus pneumoniae== | ==Structure, Function, Stability and Knockout Phenotype of Dihydrodipicolinate Synthase from Streptococcus pneumoniae== | ||
<StructureSection load='3vfl' size='340' side='right' caption='[[3vfl]], [[Resolution|resolution]] 1.91Å' scene=''> | <StructureSection load='3vfl' size='340' side='right' caption='[[3vfl]], [[Resolution|resolution]] 1.91Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CGSSp3BS71_00085, dapA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=406556 Streptococcus pneumoniae SP3-BS71])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CGSSp3BS71_00085, dapA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=406556 Streptococcus pneumoniae SP3-BS71])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.3.7 4.3.3.7] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.3.7 4.3.3.7] </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=3vfl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vfl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vfl RCSB], [http://www.ebi.ac.uk/pdbsum/3vfl PDBsum]</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=3vfl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vfl OCA], [http://pdbe.org/3vfl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vfl RCSB], [http://www.ebi.ac.uk/pdbsum/3vfl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vfl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3vfl" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 02:41, 5 August 2016
Structure, Function, Stability and Knockout Phenotype of Dihydrodipicolinate Synthase from Streptococcus pneumoniaeStructure, Function, Stability and Knockout Phenotype of Dihydrodipicolinate Synthase from Streptococcus pneumoniae
Structural highlights
Function[A5LD17_STREE] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) (By similarity).[HAMAP-Rule:MF_00418][SAAS:SAAS005263_004_011311] Publication Abstract from PubMedDihydrodipicolinate synthase (DHDPS; EC 4.2.1.52) catalyzes the rate-limiting step in the (S)-lysine biosynthesis pathway of bacteria and plants. Here, the cloning of the DHDPS gene from a clinical isolate of Streptococcus pneumoniae (OXC141 strain) and the strategy used to express, purify and crystallize the recombinant enzyme are described. Diffracting crystals were grown in high-molecular-weight PEG precipitants using the hanging-drop vapour-diffusion method. The best crystal, from which data were collected, diffracted to beyond 2.0 A resolution. Initially, the crystals were thought to belong to space group P4(2)2(1)2, with unit-cell parameters a = 105.5, b = 105.5, c = 62.4 A. However, the R factors remained high following initial processing of the data. It was subsequently shown that the data set was twinned and it was thus reprocessed in space group P2, resulting in a significant reduction in the R factors. Determination of the structure will provide insight into the design of novel antimicrobial agents targeting this important enzyme from S. pneumoniae. Crystallization of dihydrodipicolinate synthase from a clinical isolate of Streptococcus pneumoniae.,Sibarani NE, Gorman MA, Dogovski C, Parker MW, Perugini MA Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt, 1):32-6. Epub 2009 Dec 25. PMID:20057065[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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