Structural and computational studies of the maleate isomerase from Pseudomonas putida S16 reveal a breathing motion wrapping the substrate inside

Molecular Microbiology

Volumn 87, Issue 6, 2013, Pages 1237-1244

  Chen, Duoduo ^a   Tang, Hongzhi ^a   Lv, Yang ^a   Zhang, Zhenyi ^a   Shen, Kunlong ^a   Lin, Kui ^a   Zhao, Yi Lei ^a   Wu, Geng ^a   Xu, Ping ^a  

^a Shanghai Jiao Tong University   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ISOMERASE; MALEATE ISOMERASE; MALEIC ACID; SOLVENT; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; MOLECULAR DYNAMICS; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PSEUDOMONAS PUTIDA; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS;

BACTERIAL PROTEINS; BIOTRANSFORMATION; CIS-TRANS-ISOMERASES; CRYSTALLOGRAPHY, X-RAY; DNA MUTATIONAL ANALYSIS; FUMARATES; MALATES; MOLECULAR DYNAMICS SIMULATION; PROTEIN BINDING; PROTEIN CONFORMATION; PSEUDOMONAS PUTIDA;

NICOTIANA TABACUM; PSEUDOMONAS; PSEUDOMONAS PUTIDA;

EID: 84875000153     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12163     Document Type: Article

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