4xrr: Difference between revisions
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<StructureSection load='4xrr' size='340' side='right' caption='[[4xrr]], [[Resolution|resolution]] 2.55Å' scene=''> | <StructureSection load='4xrr' size='340' side='right' caption='[[4xrr]], [[Resolution|resolution]] 2.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xrr]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4wb1 4wb1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XRR FirstGlance]. <br> | <table><tr><td colspan='2'>[[4xrr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_15837 Atcc 15837]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4wb1 4wb1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XRR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XRR FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">calS8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1877 ATCC 15837])</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=4xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xrr OCA], [http://pdbe.org/4xrr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xrr RCSB], [http://www.ebi.ac.uk/pdbsum/4xrr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xrr 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=4xrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xrr OCA], [http://pdbe.org/4xrr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xrr RCSB], [http://www.ebi.ac.uk/pdbsum/4xrr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xrr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Classical UDP-glucose 6-dehydrogenases (UGDHs; EC 1.1.1.22) catalyze the conversion of UDP-alpha-d-glucose (UDP-Glc) to the key metabolic precursor UDP-alpha-d-glucuronic acid (UDP-GlcA) and display specificity for UDP-Glc. The fundamental biochemical and structural study of the UGDH homolog CalS8 encoded by the calicheamicin biosynthetic gene is reported and represents one of the first studies of a UGDH homolog involved in secondary metabolism. The corresponding biochemical characterization of CalS8 reveals CalS8 as one of the first characterized base-permissive UGDH homologs with a >15-fold preference for TDP-Glc over UDP-Glc. The corresponding structure elucidations of apo-CalS8 and the CalS8.substrate.cofactor ternary complex (at 2.47 and 1.95 A resolution, respectively) highlight a notably high degree of conservation between CalS8 and classical UGDHs where structural divergence within the intersubunit loop structure likely contributes to the CalS8 base permissivity. As such, this study begins to provide a putative blueprint for base specificity among sugar nucleotide-dependent dehydrogenases and, in conjunction with prior studies on the base specificity of the calicheamicin aminopentosyltransferase CalG4, provides growing support for the calicheamicin aminopentose pathway as a TDP-sugar-dependent process. | |||
Structural Characterization of CalS8, a TDP-alpha-D-Glucose Dehydrogenase Involved in Calicheamicin Aminodideoxypentose Biosynthesis.,Singh S, Michalska K, Bigelow L, Endres M, Kharel MK, Babnigg G, Yennamalli RM, Bingman CA, Joachimiak A, Thorson JS, Phillips GN Jr J Biol Chem. 2015 Oct 23;290(43):26249-58. doi: 10.1074/jbc.M115.673459. Epub, 2015 Aug 3. PMID:26240141<ref>PMID:26240141</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4xrr" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 15837]] | |||
[[Category: Babnigg, G]] | [[Category: Babnigg, G]] | ||
[[Category: Bigelow, L]] | [[Category: Bigelow, L]] | ||
Revision as of 10:31, 8 November 2017
Crystal structure of cals8 from micromonospora echinospora (P294S mutant)Crystal structure of cals8 from micromonospora echinospora (P294S mutant)
Structural highlights
Publication Abstract from PubMedClassical UDP-glucose 6-dehydrogenases (UGDHs; EC 1.1.1.22) catalyze the conversion of UDP-alpha-d-glucose (UDP-Glc) to the key metabolic precursor UDP-alpha-d-glucuronic acid (UDP-GlcA) and display specificity for UDP-Glc. The fundamental biochemical and structural study of the UGDH homolog CalS8 encoded by the calicheamicin biosynthetic gene is reported and represents one of the first studies of a UGDH homolog involved in secondary metabolism. The corresponding biochemical characterization of CalS8 reveals CalS8 as one of the first characterized base-permissive UGDH homologs with a >15-fold preference for TDP-Glc over UDP-Glc. The corresponding structure elucidations of apo-CalS8 and the CalS8.substrate.cofactor ternary complex (at 2.47 and 1.95 A resolution, respectively) highlight a notably high degree of conservation between CalS8 and classical UGDHs where structural divergence within the intersubunit loop structure likely contributes to the CalS8 base permissivity. As such, this study begins to provide a putative blueprint for base specificity among sugar nucleotide-dependent dehydrogenases and, in conjunction with prior studies on the base specificity of the calicheamicin aminopentosyltransferase CalG4, provides growing support for the calicheamicin aminopentose pathway as a TDP-sugar-dependent process. Structural Characterization of CalS8, a TDP-alpha-D-Glucose Dehydrogenase Involved in Calicheamicin Aminodideoxypentose Biosynthesis.,Singh S, Michalska K, Bigelow L, Endres M, Kharel MK, Babnigg G, Yennamalli RM, Bingman CA, Joachimiak A, Thorson JS, Phillips GN Jr J Biol Chem. 2015 Oct 23;290(43):26249-58. doi: 10.1074/jbc.M115.673459. Epub, 2015 Aug 3. PMID:26240141[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Atcc 15837
- Babnigg, G
- Bigelow, L
- Bingman, C A
- Endres, M
- Joachimiak, A
- Kharel, M K
- Structural genomic
- Michalska, K
- NatPro, Enzyme Discovery for Natural Product Biosynthesis
- Phillips, G N
- Singh, S
- Thorson, J S
- Yennamalli, R M
- Calicheamicin
- Enzyme discovery for natural product biosynthesis
- Mcsg
- Natpro
- Oxidoreductase
- Psi-biology