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Structure paper

TitleStructural basis for substrate binding and catalysis of branching enzyme from Cyanothece sp. ATCC 51142
Journal, issue, pagesTo be published
Publish dateAug 8, 2016 (structure data deposition date)
AuthorsHayashi, M. / Suzuki, R. / Colleoni, C. / Ball, S.G. / Fujita, N. / Suzuki, E.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.85 - 2.6 Å
Structure data

PDB-5gqy:
Crystal structure of branching enzyme from Cyanothece sp. ATCC 51142 in complex with maltoheptaose
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-5gqz:
Crystal structure of branching enzyme Y500A mutant from Cyanothece sp. ATCC 51142
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-5gr0:
Crystal structure of branching enzyme D501A mutant from Cyanothece sp. ATCC 51142
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-5gr1:
Crystal structure of branching enzyme Y500A/D501A mutant from Cyanothece sp. ATCC 51142 in complex with maltoheptaose
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-5gr2:
Crystal structure of branching enzyme L541A mutant from Cyanothece sp. ATCC 51142
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-5gr3:
Crystal structure of branching enzyme L541A/W655A mutant from Cyanothece sp. ATCC 51142
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-5gr4:
Crystal structure of branching enzyme L541A mutant from Cyanothece sp. ATCC 51142 in complex with maltoheptaose
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-5gr5:
Crystal structure of branching enzyme W610A mutant from Cyanothece sp. ATCC 51142
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-5gr6:
Crystal structure of branching enzyme Y500A/D501A double mutant from Cyanothece sp. ATCC 51142
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • cyanothece sp. (strain atcc 51142) (bacteria)
KeywordsTRANSFERASE / branching enzyme / glycoside hydrolase family 13 / cyanobacteria / starch

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