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5itv
From Proteopedia
(Difference between revisions)
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<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. 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 [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> |
</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='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> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5itw|5itw]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5itw|5itw]]</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='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> | <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> | ||
<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> | <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> | ||
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== 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> | [[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| + | |||
| + | 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> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5itv" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacsu]] | ||
[[Category: Dihydroanticapsin 7-dehydrogenase]] | [[Category: Dihydroanticapsin 7-dehydrogenase]] | ||
[[Category: Balaram, H]] | [[Category: Balaram, H]] | ||
Revision as of 07:36, 6 December 2017
Crystal structure of Bacillus subtilis BacC Dihydroanticapsin 7-dehydrogenase in complex with NADH
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