1UBE

MsRecA-ADP Complex

Summary for 1UBE

• Entry DOI: 10.2210/pdb1ube/pdb
• Related: 1UBC 1UBF 1UBG 1g19 1mo3
• Descriptor: RecA, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: recombination, dna-repair
• Biological source: Mycobacterium smegmatis
• Cellular location: Cytoplasm (By similarity): Q59560
• Total number of polymer chains: 1
• Total formula weight: 37771.69

Authors

Datta, S.,Krishna, R.,Ganesh, N.,Chandra, N.R.,Muniyappa, K.,Vijayan, M. (deposition date: 2003-04-04, release date: 2003-07-22, Last modification date: 2023-10-25)

Primary citation

Datta, S.,Krishna, R.,Ganesh, N.,Chandra, N.R.,Muniyappa, K.,Vijayan, M.
Crystal Structures of Mycobacterium smegmatis RecA and Its Nucleotide Complexes
J.BACTERIOL., 185:4280-4284, 2003

PubMed Abstract: The crystal structures of Mycobacterium smegmatis RecA (RecA(Ms)) and its complexes with ADP, ATPgammaS, and dATP show that RecA(Ms) has an expanded binding site like that in Mycobacterium tuberculosis RecA, although there are small differences between the proteins in their modes of nucleotide binding. Nucleotide binding is invariably accompanied by the movement of Gln 196, which appears to provide the trigger for transmitting the effect of nucleotide binding to the DNA-binding loops. These observations provide a framework for exploring the known properties of the RecA proteins.

PubMed: 12837805
DOI: 10.1128/JB.185.14.4280-4284.2003

Experimental method

X-RAY DIFFRACTION (3.3 Å)