1H1X
Sperm whale Myoglobin mutant T67R S92D
Summary for 1H1X
| Entry DOI | 10.2210/pdb1h1x/pdb |
| Related | 101M 102M 103M 104M 105M 106M 107M 108M 109M 110M 111M 112M 1A6G 1A6K 1A6M 1A6N 1ABS 1AJG 1AJH 1BVC 1BVD 1BZ6 1BZP 1BZR 1CH1 1CH2 1CH3 1CH5 1CH7 1CH9 1CIK 1CIO 1CO8 1CO9 1CP0 1CP5 1CPW 1CQ2 1DO1 1DO3 1DO4 1DO7 1DTI 1DTM 1DUK 1DUO 1DXC 1DXD 1EBC 1F63 1F65 1FCS 1HJT 1IOP 1IRC 1JDO 1JP6 1JP8 1JP9 1JPB 1JW8 1LTW 1MBC 1MBD 1MBI 1MBN 1MBO 1MCY 1MGN 1MLF 1MLG 1MLH 1MLJ 1MLK 1MLL 1MLM 1MLN 1MLO 1MLQ 1MLR 1MLS 1MLU 1MOA 1MOB 1MOC 1MOD 1MTI 1MTJ 1MTK 1MYF 1MYM 1OBM 1OFJ 1OFK 1SPE 1SWM 1TES 1VXA 1VXB 1VXC 1VXD 1VXE 1VXF 1VXG 1VXH 1YOG 1YOH 1YOI 2CMM 2MB5 2MBW 2MGA 2MGB 2MGC 2MGD 2MGE 2MGF 2MGG 2MGH 2MGI 2MGJ 2MGK 2MGL 2MGM 2MYA 2MYB 2MYC 2MYD 2MYE 2SPL 2SPM 2SPN 2SPO 4MBN 5MBN |
| Descriptor | MYOGLOBIN, PROTOPORPHYRIN IX CONTAINING FE, CYANIDE ION, ... (5 entities in total) |
| Functional Keywords | oxygen transport, globin, peroxidase, oxygen storage, heme, muscle |
| Biological source | PHYSETER CATODON (SPERM WHALE) |
| Total number of polymer chains | 1 |
| Total formula weight | 18187.83 |
| Authors | Zuccotti, S.,Bolognesi, M. (deposition date: 2002-07-25, release date: 2003-10-23, Last modification date: 2023-12-13) |
| Primary citation | Roncone, R.,Monzani, E.,Murtas, M.,Battaini, G.,Pennati, A.,Sanangelantoni, A.M.,Zuccotti, S.,Bolognesi, M.,Casella, L. Engineering Peroxidase Activity in Myoglobin: The Haem Cavity Structure and Peroxide Activation in the T67R/S92D Mutant and its Derivative Reconstituted with Protohaemin-L-Histidine. Biochem.J., 377:717-, 2004 Cited by PubMed Abstract: Atomic co-ordinates and structure factors for the T67R/S92D metMbCN mutant have been deposited with the Protein Data Bank, under accession codes 1h1x and r1h1xsf, respectively. Protein engineering and cofactor replacement have been employed as tools to introduce/modulate peroxidase activity in sperm whale Mb (myoglobin). Based on the rationale that haem peroxidase active sites are characterized by specific charged residues, the Mb haem crevice has been modified to host a haem-distalpropionate Arg residue and a proximal Asp, yielding the T67R/S92D Mb mutant. To code extra conformational mobility around the haem, and to increase the peroxidase catalytic efficiency, the T67R/S92D Mb mutant has been subsequently reconstituted with protohaem-L-histidine methyl ester, yielding a stable derivative, T67R/S92D Mb-H. The crystal structure of T67R/S92D cyano-metMb (1.4 A resolution; R factor, 0.12) highlights a regular haem-cyanide binding mode, and the role for the mutated residues in affecting the haem propionates as well as the neighbouring water structure. The conformational disorder of the haem propionate-7 is evidenced by the NMR spectrum of the mutant. Ligand-binding studies show that the iron(III) centres of T67R/S92D Mb, and especially of T67R/S92D Mb-H, exhibit higher affinity for azide and imidazole than wild-type Mb. In addition, both protein derivatives react faster than wild-type Mb with hydrogen peroxide, showing higher peroxidase-like activity towards phenolic substrates. The catalytic efficiency of T67R/S92D Mb-H in these reactions is the highest so far reported for Mb derivatives. A model for the protein-substrate interaction is deduced based on the crystal structure and on the NMR spectra of protein-phenol complexes. PubMed: 14563209DOI: 10.1042/BJ20030863 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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