2vnx | pdb_00002vnx

CRYSTAL STRUCTURE OF SOYBEAN ASCORBATE PEROXIDASE MUTANT W41A AFTER EXPOSURE TO A HIGH DOSE OF X-RAYS

spinqualitylabelsall models 2vnx, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vnx is a 1 chain structure with sequence from Glycine max. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEM, NA Related: 1oaf, 2ghc, 2ghd, 2ghh, 2ghk, 2vcn, 2vcs, 1oag, 1v0h, 2cl4, 2ggn, 2ghe, 2vcf, 2vnz Activity: Oxidoreductase, with EC number 1.11.11.1 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed We have previously shown [Badyal, S. K., et al. (2006) J. Biol. Chem. 281, 24512-24520] that the distal histidine (His42) in the W41A variant of ascorbate peroxidase binds to the heme iron in the ferric form of the protein but that binding of the substrate triggers a conformational change in which His42 dissociates from the heme. In this work, we show that this conformational rearrangement also occurs upon reduction of the heme iron. Thus, we present X-ray crystallographic data to show that reduction of the heme leads to dissociation of His42 from the iron in the ferrous form of W41A; spectroscopic and ligand binding data support this observation. Structural evidence indicates that heme reduction occurs through formation of a reduced, bis-histidine-ligated species that subsequently decays by dissociation of His42 from the heme. Collectively, the data provide clear evidence that conformational movement within the same heme active site can be controlled by both ligand binding and metal oxidation state. These observations are consistent with emerging data on other, more complex regulatory and sensing heme proteins, and the data are discussed in the context of our developing views in this area. Iron oxidation state modulates active site structure in a heme peroxidase(,).,Badyal SK, Metcalfe CL, Basran J, Efimov I, Moody PC, Raven EL Biochemistry. 2008 Apr 15;47(15):4403-9. Epub 2008 Mar 20. PMID:18351739 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ascorbate peroxidase

Proteopedia Page Contributors and Editors (what is this?)

OCA