2bwh | pdb_00002bwh

Laue Structure of a Short Lived State of L29W Myoglobin

spinqualitylabelsall models 2bwh, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2bwh is a 1 chain structure with sequence from Phycd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CMO, HEM 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, 2bli, 2blj, 2bw9, 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 Gene: MB (PHYCD) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MYG_PHYCD] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. 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 By using time-resolved x-ray crystallography at room temperature, structural relaxations and ligand migration were examined in myoglobin (Mb) mutant L29W from nanoseconds to seconds after photodissociation of carbon monoxide (CO) from the heme iron by nanosecond laser pulses. The data were analyzed in terms of transient kinetics by fitting trial functions to integrated difference electron density values obtained from select structural moieties, thus allowing a quantitative description of the processes involved. The observed relaxations are linked to other investigations on protein dynamics. At the earliest times, the heme has already completely relaxed into its domed deoxy structure, and there is no photo-dissociated CO visible at the primary docking site. Initial relaxations of larger globin moieties are completed within several hundred nanoseconds. They influence the concomitant migration of photo-dissociated CO to the Xe1 site, where it appears at approximately 300 ns and leaves again at approximately 1.5 ms. The extremely long residence time in Xe1 as compared with wild-type MbCO implies that, in the latter protein, the CO exits the protein from Xe1 predominantly via the distal pocket. A well-defined deligated state is populated between approximately 2 micros and approximately 1 ms; its structure is very similar to the equilibrium deoxy structure. Between 1.5 and 20 ms, no CO is visible in the protein interior; it is either distributed among many sites within the protein or has escaped to the solvent. Finally, recombination at the heme iron occurs after >20 ms. Ligand migration pathway and protein dynamics in myoglobin: a time-resolved crystallographic study on L29W MbCO.,Schmidt M, Nienhaus K, Pahl R, Krasselt A, Anderson S, Parak F, Nienhaus GU, Srajer V Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11704-9. Epub 2005 Aug 5. PMID:16085709 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Myoglobin

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