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| | <StructureSection load='6ue0' size='340' side='right'caption='[[6ue0]], [[Resolution|resolution]] 1.89Å' scene=''> | | <StructureSection load='6ue0' size='340' side='right'caption='[[6ue0]], [[Resolution|resolution]] 1.89Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ue0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pneumoniae"_(schroeter_1886)_flugge_1886 "bacillus pneumoniae" (schroeter 1886) flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UE0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UE0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ue0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UE0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.892Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KPI:(2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)AMINO]HEXANOIC+ACID'>KPI</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KPI:(2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)AMINO]HEXANOIC+ACID'>KPI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dapA_2, dapA_3, dapA_4, dapA_5, dapA_6, dapA_7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=573 "Bacillus pneumoniae" (Schroeter 1886) Flugge 1886])</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=6ue0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ue0 OCA], [https://pdbe.org/6ue0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ue0 RCSB], [https://www.ebi.ac.uk/pdbsum/6ue0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ue0 ProSAT]</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://proteopedia.org/fgij/fg.htm?mol=6ue0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ue0 OCA], [http://pdbe.org/6ue0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ue0 RCSB], [http://www.ebi.ac.uk/pdbsum/6ue0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ue0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/W9BBZ5_KLEPN W9BBZ5_KLEPN]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418][SAAS:SAAS00570606] | + | [https://www.uniprot.org/uniprot/W9BBZ5_KLEPN W9BBZ5_KLEPN] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418][SAAS:SAAS00570606] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6ue0" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6ue0" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 4-hydroxy-tetrahydrodipicolinate synthase]] | + | [[Category: Klebsiella pneumoniae]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Costa, T P.Soares da]]
| + | [[Category: Hawkins DA]] |
| - | [[Category: Hawkins, D A]] | + | [[Category: Impey RE]] |
| - | [[Category: Impey, R E]] | + | [[Category: Lee M]] |
| - | [[Category: Lee, M]] | + | [[Category: Panjikar S]] |
| - | [[Category: Panjikar, S]] | + | [[Category: Perugini MA]] |
| - | [[Category: Perugini, M A]] | + | [[Category: Soares da Costa TP]] |
| - | [[Category: Sutton, J M]] | + | [[Category: Sutton JM]] |
| - | [[Category: Dhdp]] | + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Lysine biosynthesis]]
| + | |
| - | [[Category: Tetramer]]
| + | |
| Structural highlights
Function
W9BBZ5_KLEPN Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418][SAAS:SAAS00570606]
Publication Abstract from PubMed
The rise of antibiotic resistance combined with the lack of new products entering the market has led to bacterial infections becoming one of the biggest threats to global health. Therefore, there is an urgent need to identify novel antibiotic targets, such as dihydrodipicolinate synthase (DHDPS), an enzyme involved in the production of essential metabolites in cell wall and protein synthesis. Here, we utilised a 7-residue sequence motif to identify mis-annotation of multiple DHDPS genes in the high-priority Gram-negative bacteria Acinetobacter baumannii and Klebsiella pneumoniae. We subsequently confirmed these mis-annotations using a combination of enzyme kinetics and X-ray crystallography. Thus, this study highlights the need to ensure genes encoding promising drug targets, like DHDPS, are annotated correctly, especially for clinically important pathogens. PDB ID: 6UE0.
Mis-annotations of a promising antibiotic target in high-priority gram-negative pathogens.,Impey RE, Lee M, Hawkins DA, Sutton JM, Panjikar S, Perugini MA, Soares da Costa TP FEBS Lett. 2020 Jan 13. doi: 10.1002/1873-3468.13733. PMID:31943170[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Impey RE, Lee M, Hawkins DA, Sutton JM, Panjikar S, Perugini MA, Soares da Costa TP. Mis-annotations of a promising antibiotic target in high-priority gram-negative pathogens. FEBS Lett. 2020 Jan 13. doi: 10.1002/1873-3468.13733. PMID:31943170 doi:http://dx.doi.org/10.1002/1873-3468.13733
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