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Volumn 272, Issue 5268, 1996, Pages 1615-1621

Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination

Author keywords

[No Author keywords available]

Indexed keywords

DIMETHYL SULFIDE; DINUCLEOTIDE; GUANINE; MOLYBDENUM; OXIDOREDUCTASE; PTERIN DERIVATIVE;

EID: 0030006891     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.272.5268.1615     Document Type: Article
Times cited : (451)

References (56)
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    • 1 with a = 62.00 Å, b = 75.85 Å, and c = 198.32 Å and contain one molecule per asymmetric unit.
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    • 649 being again in disallowed regions. The average coordinate error of this model is 0.25 Å.
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    • note
    • We used 95 Cα atoms for the superposition yielding an rms deviation of 2.1 Å. Structurally equivalent pairs of residues are: 86 to 100 and 300 to 314; 108 to 117 and 315 to 324; 125 to 139 and 333 to 347; 424 to 439 and 177 to 192; 448 to 451 and 210 to 213; 453 to 465 and 215 to 227; 470 to 477 and 233 to 240; and 510 to 523 and 242 to 255.
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    • note
    • We thank J. Enemark for insightful discussions and suggestions on the manuscript. Supported by Deutsche Forschungsgemeinschaft postdoctoral fellowships (to C.K. and H.S.), by USPHS grant GM50775 (D.C.R.), and by USPHS grant GM00091 (K.V.R.). The rotation camera facility at SSRL is supported by the Department of Energy and NIH. The X-PLOR calculations were performed on the CRAY C90 at the San Diego Supercomputer Center, supported by the NSF. Coordinates have been deposited in the Brookhaven Protein Data Bank and can be supplied by e-mail to hermann@citray.caltech.edu.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.