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Structure paper

TitleKinetic and X-ray structural evidence for negative cooperativity in substrate binding to nicotinate mononucleotide adenylyltransferase (NMAT) from Bacillus anthracis.
Journal, issue, pagesJ. Mol. Biol., Vol. 385, Page 867-888, Year 2009
Publish dateAug 2, 2007 (structure data deposition date)
AuthorsSershon, V.C. / Santarsiero, B.D. / Mesecar, A.D.
External linksJ. Mol. Biol. / PubMed:18977360
MethodsX-ray diffraction
Resolution1.7 - 2.4 Å
Structure data

PDB-2qtm:
Crystal Structure of Nicotinate Mononucleotide Adenylyltransferase
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-2qtn:
Crystal Structure of Nicotinate Mononucleotide Adenylyltransferase
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-2qtr:
Crystal Structure of Nicotinate Mononucleotide Adenylyltransferase
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-CO:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

ChemComp-NCN:
NICOTINATE MONONUCLEOTIDE

ChemComp-SO4:
SULFATE ION

ChemComp-DND:
NICOTINIC ACID ADENINE DINUCLEOTIDE

Source
  • bacillus anthracis (anthrax bacterium)
KeywordsTRANSFERASE / NAD / Nucleotidyltransferase / Pyridine nucleotide biosynthesis

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