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| | ==Crystal structure of Bacillus subtilis BacC Dihydroanticapsin 7-dehydrogenase in complex with NADH== | | ==Crystal structure of Bacillus subtilis BacC Dihydroanticapsin 7-dehydrogenase in complex with NADH== |
| - | <StructureSection load='5itv' size='340' side='right' caption='[[5itv]], [[Resolution|resolution]] 2.26Å' scene=''> | + | <StructureSection load='5itv' size='340' side='right'caption='[[5itv]], [[Resolution|resolution]] 2.26Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5itv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ITV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ITV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5itv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ITV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ITV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</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]] 2.26Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5itw|5itw]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bacC, ywfD, BSU37720, ipa-82d ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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=5itv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5itv OCA], [https://pdbe.org/5itv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5itv RCSB], [https://www.ebi.ac.uk/pdbsum/5itv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5itv 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/Dihydroanticapsin_7-dehydrogenase Dihydroanticapsin 7-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.385 1.1.1.385] </span></td></tr>
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| - | <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=5itv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5itv OCA], [http://pdbe.org/5itv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5itv RCSB], [http://www.ebi.ac.uk/pdbsum/5itv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5itv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BACC_BACSU BACC_BACSU]] Part of the bacABCDEFG operon responsible for the biosynthesis of bacilysin, an irreversible inactivator of the glutaminase domain of glucosamine synthetase. Catalyzes the dehydrogenation of the C7-hydroxyl group in the 4S-tetrahydrotyrosine (4S-H4Tyr) to yield anticapsin (epoxycyclohexanonyl-Ala). It is not able to oxidize the 4R-H4Tyr diastereomer and the dihydrobacilysin dipeptide (L-Ala-4S-H4Tyr dipeptide).<ref>PMID:15609023</ref> <ref>PMID:23317005</ref> | + | [https://www.uniprot.org/uniprot/BACC_BACSU BACC_BACSU] Part of the bacABCDEFG operon responsible for the biosynthesis of bacilysin, an irreversible inactivator of the glutaminase domain of glucosamine synthetase. Catalyzes the dehydrogenation of the C7-hydroxyl group in the 4S-tetrahydrotyrosine (4S-H4Tyr) to yield anticapsin (epoxycyclohexanonyl-Ala). It is not able to oxidize the 4R-H4Tyr diastereomer and the dihydrobacilysin dipeptide (L-Ala-4S-H4Tyr dipeptide).<ref>PMID:15609023</ref> <ref>PMID:23317005</ref> |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Bacillus subtilis BacC is an oxidoreductase involved in the biosynthesis of the potent antibiotic bacilysin. The crystal structure of BacC was determined at 1.19 A resolution. An experimental charge density approach was used to calculate non-covalent interactions within the monomer and across the dimeric interface of BacC. This interaction network, in turn, enabled an analysis of non-covalently connected paths that span the protein structure. One of the pathways of non-covalent interactions was examined by mutational analysis. Biochemical analysis of BacC mutants with potential disruptions in non-covalent interactions along this path revealed that residues that form nodes in pathways of non-covalent interactions influence catalytic activity more than others in a similar chemical environment. Furthermore, we note that nodes in the non-covalent interaction networks are co-localized with compensatory mutation sites identified by multiple sequence alignment of proteins with low sequence similarity to BacC. Put together, this analysis supports the hypothesis that non-covalent nodes represent conserved structural features that can impact the catalytic activity of an enzyme.
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| - | Probing the influence of non-covalent contact networks identified by charge density analysis on the oxidoreductase BacC.,Perinbam K, Balaram H, Guru Row TN, Gopal B Protein Eng Des Sel. 2017 Mar 1;30(3):265-272. doi: 10.1093/protein/gzx006. PMID:28158843<ref>PMID:28158843</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 5itv" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacsu]] | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
| - | [[Category: Dihydroanticapsin 7-dehydrogenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Balaram, H]] | + | [[Category: Balaram H]] |
| - | [[Category: Gopal, B]] | + | [[Category: Gopal B]] |
| - | [[Category: Perinbam, K]] | + | [[Category: Perinbam K]] |
| - | [[Category: Row, T N.G]] | + | [[Category: Row TNG]] |
| - | [[Category: Oxidoreductase]]
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| - | [[Category: Rossmann fold]]
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| - | [[Category: Short-chain dehydrogenases/reductase]]
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