A pH-dependent stabilization of an active site loop observed from low and high pH crystal structures of mutant monomeric glycinamide ribonucleotide transformylase at 1.8 to 1.9 Å

Journal of Molecular Biology

Volumn 281, Issue 3, 1998, Pages 485-499

  Su, Ying ^a   Yamashita, Mason M ^a   Greasley, Samantha E ^a   Mullen, Christine A ^b   Shim, Jae Hoon ^c   Jennings, Patricia A ^b   Benkovic, Steven J ^c   Wilson, Ian A ^a  

^a 92093 0359 ^*  (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c PENNSYLVANIA STATE UNIVERSITY   (United States)

Author keywords

Enzyme mechanism; Folate cofactors; Loop flexibility; Monomer dimer association; Purine biosynthesis

Indexed keywords

4 AMINOBENZOIC ACID; FOLIC ACID; OXYGEN; PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE;

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME STRUCTURE; HYDROGEN BOND; HYDROPHOBICITY; NONHUMAN; PH; PKA; PRIORITY JOURNAL;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0032555703     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1931     Document Type: Article

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