5hv0: Difference between revisions
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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=5hv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hv0 OCA], [http://pdbe.org/5hv0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hv0 RCSB], [http://www.ebi.ac.uk/pdbsum/5hv0 PDBsum]</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=5hv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hv0 OCA], [http://pdbe.org/5hv0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hv0 RCSB], [http://www.ebi.ac.uk/pdbsum/5hv0 PDBsum]</span></td></tr> | ||
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== Publication Abstract from PubMed == | |||
The prolyl 4-hydroxylases (P4Hs) are mononuclear nonheme iron enzymes that catalyze the formation of 4R-hydroxyproline from many different substrates, with various biological implications. P4H is a key player in collagen accumulation, which has implications in fibrotic disorders. The stabilization of collagen triple-helical structure via prolyl hydroxylation is the rate-limiting step in collagen biosynthesis, and therefore P4H has been extensively investigated as a potential therapeutic target of fibrotic disease. Understanding how these enzymes recognize cofactors and substrates is important and will aid in the future design of inhibitors of P4H. In this article, X-ray crystal structures of a metallocofactor- and alpha-ketoglutarate (alphaKG)-bound form of P4H from Bacillus anthracis (BaP4H) are reported. Structures of BaP4H were solved at 1.63 and 2.35 A resolution and contained a cadmium ion and alphaKG bound in the active site. The alphaKG-Cd-BaP4H ternary complex reveals conformational changes of conserved residues upon the binding of metal ion and alphaKG, resulting in a closed active-site configuration required for dioxygen, substrate binding and catalysis. | |||
Structural analysis of cofactor binding for a prolyl 4-hydroxylase from the pathogenic bacterium Bacillus anthracis.,Schnicker NJ, Dey M Acta Crystallogr D Struct Biol. 2016 May 1;72(Pt 5):675-81. doi:, 10.1107/S2059798316004198. Epub 2016 Apr 26. PMID:27139630<ref>PMID:27139630</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 5hv0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 11:16, 1 June 2016
Structural Analysis of Cofactor Binding of a Prolyl 4-Hydroxylase from the Pathogenic Bacterium Bacillus anthracisStructural Analysis of Cofactor Binding of a Prolyl 4-Hydroxylase from the Pathogenic Bacterium Bacillus anthracis
Structural highlights
Publication Abstract from PubMedThe prolyl 4-hydroxylases (P4Hs) are mononuclear nonheme iron enzymes that catalyze the formation of 4R-hydroxyproline from many different substrates, with various biological implications. P4H is a key player in collagen accumulation, which has implications in fibrotic disorders. The stabilization of collagen triple-helical structure via prolyl hydroxylation is the rate-limiting step in collagen biosynthesis, and therefore P4H has been extensively investigated as a potential therapeutic target of fibrotic disease. Understanding how these enzymes recognize cofactors and substrates is important and will aid in the future design of inhibitors of P4H. In this article, X-ray crystal structures of a metallocofactor- and alpha-ketoglutarate (alphaKG)-bound form of P4H from Bacillus anthracis (BaP4H) are reported. Structures of BaP4H were solved at 1.63 and 2.35 A resolution and contained a cadmium ion and alphaKG bound in the active site. The alphaKG-Cd-BaP4H ternary complex reveals conformational changes of conserved residues upon the binding of metal ion and alphaKG, resulting in a closed active-site configuration required for dioxygen, substrate binding and catalysis. Structural analysis of cofactor binding for a prolyl 4-hydroxylase from the pathogenic bacterium Bacillus anthracis.,Schnicker NJ, Dey M Acta Crystallogr D Struct Biol. 2016 May 1;72(Pt 5):675-81. doi:, 10.1107/S2059798316004198. Epub 2016 Apr 26. PMID:27139630[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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