3si9
From Proteopedia
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==Crystal structure of Dihydrodipicolinate Synthase from Bartonella Henselae== | ==Crystal structure of Dihydrodipicolinate Synthase from Bartonella Henselae== | ||
<StructureSection load='3si9' size='340' side='right' caption='[[3si9]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='3si9' size='340' side='right' caption='[[3si9]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3si9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3si9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_49882 Atcc 49882]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SI9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SI9 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dapA, BH05000 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=38323 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dapA, BH05000 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=38323 ATCC 49882])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ | + | <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=3si9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3si9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3si9 RCSB], [http://www.ebi.ac.uk/pdbsum/3si9 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=3si9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3si9 OCA], [http://pdbe.org/3si9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3si9 RCSB], [http://www.ebi.ac.uk/pdbsum/3si9 PDBsum]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/DAPA_BARHE DAPA_BARHE]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418] | [[http://www.uniprot.org/uniprot/DAPA_BARHE DAPA_BARHE]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The enzyme dihydrodipicolinate synthase catalyzes the committed step in the synthesis of diaminopimelate and lysine to facilitate peptidoglycan and protein synthesis. Dihydrodipicolinate synthase catalyzes the condensation of L-aspartate 4-semialdehyde and pyruvate to synthesize L-2,3-dihydrodipicolinate. Here, the cloning, expression, purification, crystallization and X-ray diffraction analysis of dihydrodipicolinate synthase from the pathogenic bacterium Bartonella henselae, the causative bacterium of cat-scratch disease, are presented. Protein crystals were grown in conditions consisting of 20%(w/v) PEG 4000, 100 mM sodium citrate tribasic pH 5.5 and were shown to diffract to approximately 2.10 A resolution. They belonged to space group P212121, with unit-cell parameters a = 79.96, b = 106.33, c = 136.25 A. The final R values were Rr.i.m. = 0.098, Rwork = 0.183, Rfree = 0.233. | ||
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| + | Cloning, expression, purification, crystallization and X-ray diffraction analysis of dihydrodipicolinate synthase from the human pathogenic bacterium Bartonella henselae strain Houston-1 at 2.1 A resolution.,Naqvi KF, Staker BL, Dobson RC, Serbzhinskiy D, Sankaran B, Myler PJ, Hudson AO Acta Crystallogr F Struct Biol Commun. 2016 Jan 1;72(Pt 1):2-9. doi:, 10.1107/S2053230X15023213. Epub 2016 Jan 1. PMID:26750477<ref>PMID:26750477</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3si9" 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: 4-hydroxy-tetrahydrodipicolinate synthase]] |
| - | [[Category: | + | [[Category: Atcc 49882]] |
[[Category: Abendroth, J]] | [[Category: Abendroth, J]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
Revision as of 06:49, 2 March 2016
Crystal structure of Dihydrodipicolinate Synthase from Bartonella Henselae
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