Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3ZCG

Ascorbate peroxidase W41A-H42C mutant

Summary for 3ZCG
Entry DOI10.2210/pdb3zcg/pdb
Related3ZCH
DescriptorASCORBATE PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (6 entities in total)
Functional Keywordsoxidoreductase, conformational mobility
Biological sourceGLYCINE MAX (SOYBEAN)
Total number of polymer chains1
Total formula weight29297.79
Authors
Gumiero, A.,Raven, E.L.,Moody, P.C.E. (deposition date: 2012-11-20, release date: 2012-12-19, Last modification date: 2023-12-20)
Primary citationGuimero, A.,Badyal, S.K.,Leeks, T.,Moody, P.C.E.,Raven, E.L.
Probing the Conformational Mobility of the Active Site of a Heme Peroxidase.
Dalton Trans, 42:3170-, 2013
Cited by
PubMed Abstract: We have previously demonstrated (Badyal et al., J. Biol. Chem., 2006, 281, 24512) that removal of the active site tryptophan (Trp41) in ascorbate peroxidase increases the conformational mobility of the distal histidine residue (His42) and that His42 coordinates to the iron in the oxidised W41A enzyme to give a 6-coordinate, low-spin peroxidase. In this work, we probe the conformational flexibility of the active site in more detail. We examine whether other residues (Cys, Tyr, Met) can also ligate to the heme at position 42; we find that introduction of other ligating amino acids created a cavity in the heme pocket, but that formation of 6-coordinate heme is not observed. In addition, we examine the role of Asn-71, which hydrogen bonds to His42 and tethers the distal histidine in the active site pocket; we find that removal of this hydrogen bond increases the proportion of low-spin heme. We suggest that, in addition to its well-known role in facilitating the reaction with peroxide, His42 also plays a role in defining the shape and folding of the active site pocket.
PubMed: 23202589
DOI: 10.1039/C2DT32455E
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.491 Å)
Structure validation

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon