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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/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> | + | <table><tr><td colspan='2'>[[3si9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bartonella_henselae Bartonella henselae]. 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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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 ATCC 49882])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=3si9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3si9 OCA], [https://pdbe.org/3si9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3si9 RCSB], [https://www.ebi.ac.uk/pdbsum/3si9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3si9 ProSAT]</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] | + | [https://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;">
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| - | == Publication Abstract from PubMed ==
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| - | 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>
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| - | </div>
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| - | <div class="pdbe-citations 3si9" style="background-color:#fffaf0;"></div>
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| | ==See Also== | | ==See Also== |
| | *[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]] | | *[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]] |
| - | == References == | |
| - | <references/> | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 4-hydroxy-tetrahydrodipicolinate synthase]] | + | [[Category: Bartonella henselae]] |
| - | [[Category: Atcc 49882]] | + | [[Category: Large Structures]] |
| - | [[Category: Abendroth, J]] | + | [[Category: Abendroth J]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Sankaran B]] |
| - | [[Category: Sankaran, B]] | + | [[Category: Staker BL]] |
| - | [[Category: Staker, B L]] | + | |
| - | [[Category: Lyase]]
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| - | [[Category: Ssgcid]]
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| - | [[Category: Tim barrel]]
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