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Structure paper

TitleSubstrate and Product Complexes of Escherichia coli Adenylosuccinate Lyase Provide New Insights into the Enzymatic Mechanism.
Journal, issue, pagesJ. Mol. Biol., Vol. 370, Page 541-554, Year 2007
Publish dateMay 8, 2007 (structure data deposition date)
AuthorsTsai, M. / Koo, J. / Yip, P. / Colman, R.F. / Segall, M.L. / Howell, P.L.
External linksJ. Mol. Biol. / PubMed:17531264
MethodsX-ray diffraction
Resolution1.85 - 2 Å
Structure data

PDB-2ptq:
Crystal structure of Escherichia coli adenylosuccinate lyase mutant H171N with bound AMP and fumarate
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-2ptr:
Crystal structure of Escherichia coli adenylosuccinate lyase mutant H171A with bound adenylosuccinate substrate
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-2pts:
Crystal structure of wild type Escherichia coli adenylosuccinate lyase
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-FUM:
FUMARIC ACID

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-HOH:
WATER

ChemComp-2SA:
2-[9-(3,4-DIHYDROXY-5-PHOSPHONOOXYMETHYL-TETRAHYDRO-FURAN-2-YL)-9H-PURIN-6-YLAMINO]-SUCCINIC ACID

Source
  • escherichia coli (E. coli)
KeywordsLYASE / adenylosuccinate lyase / mutant-product complex / mutant-substrate complex / wild-type-selenomethionine substituted

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