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Structure paper

TitleIs the Critical Role of Loop 3 of Escherichia coli 6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase in Catalysis Due to Loop-3 Residues Arginine-84 and Tryptophan-89? Site-Directed Mutagenesis, Biochemical, and Crystallographic Studies.
Journal, issue, pagesBiochemistry, Vol. 44, Page 8590-8599, Year 2005
Publish dateJun 10, 2004 (structure data deposition date)
AuthorsLi, Y. / Blaszczyk, J. / Wu, Y. / Shi, G. / Ji, X. / Yan, H.
External linksBiochemistry / PubMed:15952765
MethodsX-ray diffraction
Resolution1.25 - 1.45 Å
Structure data

PDB-1tmj:
Crystal structure of E.coli apo-HPPK(W89A) at 1.45 Angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

PDB-1tmm:
Crystal structure of ternary complex of E.coli HPPK(W89A) with MGAMPCPP and 6-Hydroxymethylpterin
Method: X-RAY DIFFRACTION / Resolution: 1.25 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-ACT:
ACETATE ION

ChemComp-APC:
DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER / AMP-CPP, energy-carrying molecule analogue*YM

ChemComp-HHR:
6-HYDROXYMETHYLPTERIN

ChemComp-GOL:
GLYCEROL

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / PYROPHOSPHOKINASE / PYROPHOSPHORYL TRANSFER / FOLATE / HPPK / 6-HYDROXYMETHYLPTERIN / 6-HYDROXYMETHYL-7 / 8-DIHYDROPTERIN / ANTIMICROBIAL AGENT / DRUG DESIGN / POINT MUTANT / STRUCTURAL MUTAGENESIS / CATALYTIC MECHANISM / PTERIN / TERNARY COMPLEX / SUBSTRATE SPECIFICITY / PRODUCT RELEASE

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