|
Volumn 41, Issue 2, 2002, Pages 521-529
|
GTP hydrolysis of cell division protein FtsZ: Evidence that the active site is formed by the association of monomers
|
Author keywords
[No Author keywords available]
|
Indexed keywords
MUTATIONS;
ESCHERICHIA COLI;
HYDROLYSIS;
MONOMERS;
MUTAGENESIS;
POLYMERIZATION;
POLYMERS;
PROTEINS;
CELLS;
GUANOSINE TRIPHOSPHATE;
ANIMAL CELL;
ARTICLE;
CELL DIVISION;
CHLOROPLAST;
CRYSTAL STRUCTURE;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
HYDROLYSIS;
NONHUMAN;
POLYMERIZATION;
PRIORITY JOURNAL;
PROKARYOTE;
PROTEIN LOCALIZATION;
PROTEIN SYNTHESIS INHIBITION;
STRUCTURE ANALYSIS;
AMINO ACID SEQUENCE;
BACTERIAL PROTEINS;
BINDING SITES;
CALCIUM;
CYSTEINE;
CYTOSKELETAL PROTEINS;
DOSE-RESPONSE RELATIONSHIP, DRUG;
ESCHERICHIA COLI;
GLUTAMIC ACID;
GTP PHOSPHOHYDROLASES;
GUANOSINE TRIPHOSPHATE;
HYDROLYSIS;
LIGHT;
MAGNESIUM;
MICROSCOPY, ELECTRON;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
MUTATION;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN STRUCTURE, TERTIARY;
SCATTERING, RADIATION;
SEQUENCE HOMOLOGY, AMINO ACID;
TIME FACTORS;
ANIMALIA;
ESCHERICHIA COLI;
PROKARYOTA;
|
EID: 0037080162
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi011370i Document Type: Article |
Times cited : (137)
|
References (44)
|