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Structure paper

TitleAntenna Domain Mobility and Enzymatic Reaction of L-Rhamnulose-1-Phosphate Aldolase.
Journal, issue, pagesBiochemistry, Vol. 47, Page 607-, Year 2008
Publish dateJun 4, 2007 (structure data deposition date)
AuthorsGrueninger, D. / Schulz, G.E.
External linksBiochemistry / PubMed:18085797
MethodsX-ray diffraction
Resolution1.5 - 2 Å
Structure data

PDB-2v29:
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT K15W)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-2v2a:
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A- K248G-R253A-E254A)
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-2v2b:
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E117S- E192A-K248G-R253A-E254A)
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-13P:
1,3-DIHYDROXYACETONEPHOSPHATE

ChemComp-PGR:
R-1,2-PROPANEDIOL

ChemComp-PO4:
PHOSPHATE ION

Source
  • escherichia coli (E. coli)
KeywordsLYASE / ZINC ENZYME / METAL-BINDING / SURFACE MUTATION / 2-KETOSE DEGRADATION / PROTEIN-PROTEIN INTERFACE / ALDOLASE / CLASS II / RARE SUGAR / CLEAVAGE OF L-RHAMNULOSE-1-PHOSPHATE TO DIHYDROXYACETONE PHOSPHATE / BACTERIAL L-RHAMNOSE METABOLISM / RHAMNOSE METABOLISM / PROTEIN ENGINEERING / DOMAIN MOTION FOR MECHANICAL SUPPORT OF CATALYSIS

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