2BLI
L29W Mb deoxy
Summary for 2BLI
| Entry DOI | 10.2210/pdb2bli/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 1F6H 1FCS 1H1X 1HJT 1IOP 1IRC 1J3F 1J52 1JDO 1JP6 1JP8 1JP9 1JPB 1JW8 1L2K 1LTW 1LUE 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 1MYZ 1MZ0 1N9F 1N9H 1N9I 1N9X 1NAZ 1O16 1OBM 1OFJ 1OFK 1SPE 1SWM 1TES 1UFJ 1UFP 1VXA 1VXB 1VXC 1VXD 1VXE 1VXF 1VXG 1VXH 1WVP 1YOG 1YOH 1YOI 2BLH 2BLJ 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 (3 entities in total) |
| Functional Keywords | myoglobin, mutant, oxygen transport, heme |
| Biological source | PHYSETER CATODON (SPERM WHALE) |
| Total number of polymer chains | 1 |
| Total formula weight | 17923.51 |
| Authors | Nienhaus, K.,Ostermann, A.,Nienhaus, G.U.,Parak, F.G.,Schmidt, M. (deposition date: 2005-03-04, release date: 2005-04-06, Last modification date: 2024-05-08) |
| Primary citation | Nienhaus, K.,Ostermann, A.,Nienhaus, G.U.,Parak, F.G.,Schmidt, M. Ligand Migration and Protein Fluctuations in Myoglobin Mutant L29W Biochemistry, 44:5095-, 2005 Cited by PubMed Abstract: We have determined eight X-ray structures of myoglobin mutant L29W at various experimental conditions. In addition, infrared spectroscopic experiments are presented, which are discussed in the light of the X-ray structures. Two distinct conformations of the CO-ligated protein were identified, giving rise to two stretching bands of heme-bound CO. If L29W MbCO crystals are illuminated around 180 K, a deoxy species is formed. The CO molecules migrate to the proximal side of the heme and remain trapped in the so-called Xe1 cavity upon temperature decrease to 105 K. The structure of this photoproduct is almost identical to the equilibrium high-temperature deoxy Mb structure. If the temperature is cycled to increasingly higher values, CO recombination is observed. Three intermediate structures have been determined during the rebinding process. Efficient recombination occurs only above 180 K, the characteristic temperature for the onset of protein dynamics. Rebinding is remarkably slow because bulky residues His64 and Trp29 block important migration pathways of the CO molecule. PubMed: 15794647DOI: 10.1021/BI047513T PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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