3vfl
From Proteopedia
(Difference between revisions)
(One intermediate revision not shown.) | |||
Line 1: | Line 1: | ||
==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=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3vfl]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3vfl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_SP3-BS71 Streptococcus pneumoniae SP3-BS71]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3h5d 3h5d]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VFL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VFL FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.91Å</td></tr> |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr> | |
- | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vfl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vfl OCA], [https://pdbe.org/3vfl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vfl RCSB], [https://www.ebi.ac.uk/pdbsum/3vfl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vfl ProSAT]</span></td></tr> |
- | < | + | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
- | == Function == | ||
- | [[http://www.uniprot.org/uniprot/A5LD17_STREE 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] | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | Dihydrodipicolinate 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<ref>PMID:20057065</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 3vfl" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]] | *[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Streptococcus pneumoniae | + | [[Category: Streptococcus pneumoniae SP3-BS71]] |
- | [[Category: Gorman | + | [[Category: Gorman MA]] |
- | + | ||
- | + | ||
- | + |
Current revision
Structure, Function, Stability and Knockout Phenotype of Dihydrodipicolinate Synthase from Streptococcus pneumoniae
|