1MO6	Hydrolase	date	Sep 07, 2002
title	Reca-Datp-Mg Complex
authors	S.Datta, N.Ganesh, N.R.Chandra, Tb Structural Genomics Consortium (Tbsgc)
compound		source
Molecule: Reca Chain: A Synonym: Recombinase A Ec: 3.4.99.37 Engineered: Yes		Organism_scientific: Mycobacterium Tuberculosis Organism_common: Bacteria Expression_system: Escherichia Coli Expression_system_common: Bacteria Expression_system_strain: Km4104 Expression_system_vector_type: Plasmid Expression_system_plasmid: Pej135
symmetry	Space Group: P 61	R_factor	0.189
crystal cell	length a length b length c angle alpha angle beta angle gamma 108.077 108.077 72.361 90.00 90.00 120.00
method	X-Ray Diffraction	resolution	3.20 Å
ligand	DTP	enzyme	Hydrolase E.C.3.4.99.37 BRENDA
similarity	Belongs to the RecA family. Contains 1 dod-type homing endonuclease domain.
post-translat. modifications	This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation.
subcellular loc.	Cytoplasm (by similarity).
genes	MT2806, recA (M. tuberculosis)
function	Pi-mtui is an endonuclease. Can catalyze the hydrolysis of atp in the presence of single-stranded dna, the atp-dependent uptake of single-stranded dna by duplex dna, and the atp-dependent hybridization of homologous single-stranded dnas. It interacts with lexa causing its activation and leading to its autocatalytic cleavage.
Gene Ontology	Chain Function Process Component A nucleotide binding DNA binding damaged DNA binding single-stranded DNA binding nuclease activity endonuclease activity ATP binding DNA-dependent ATPase activit... hydrolase activity nucleoside-triphosphatase ac... DNA metabolic process DNA repair DNA recombination intron homing response to DNA damage stimu... SOS response intein-mediated protein spli... protein splicing
Primary reference	Structural studies on MtRecA-nucleotide complexes: insights into DNA and nucleotide binding and the structural signature of NTP recognition., Datta S, Ganesh N, Chandra NR, Muniyappa K, Vijayan M, Proteins 2003 Feb 15;50(3):474-85. PMID:12557189

Data retrieval

Asymmetric unit, PDB entry: [header only] [complete with coordinates] (62 Kb) [Save to disk] Biological Unit Coordinates (1mo6.pdb1.gz) 46 Kb CSU: Contacts of Structural Units for 1MO6 Likely Quarternary Molecular Structure file(s) for 1MO6 Structure Factors (65 Kb) Retrieve 1MO6 in mmCIF format [Save to disk]

View 1MO6 in 3D

On Jmol, a nice Rasmol like molecule viewer. This is good for easiest viewing of basic structure. On FirstGlance, an excellent tool for a guided tour on the structure components, by E. Martz. On AstexViewer, from MSD-EBI (viewer documentation). On RasMol (Install RasMol freeware) Here's help on how to use RasMol.

Visual 3D analysis of 1MO6

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Structure-derived information

Electron Density related parameters from EDS Electron Density Server, at Upsala Dipole moment, from Dipole Server at Weizmann Institute Crystal Contacts, from CryCo at Weizmann Institute 3D motif for 1MO6, from MSDmotif at EBI Classification of representative domains in scop (Structural Classification of Proteins)     - Domain d1mo6a1, region A:1-269 [Jmol] [rasmolscript] [script source]     - Domain d1mo6a2, region A:270-329 [Jmol] [rasmolscript] [script source] Fold representative 1mo6 from FSSP and Dali (Families of Structurally Similar Proteins) Class (fold), Architecture (subfold), Topology, Homologous superfamily from CATH Summaries and structural analyses of PDB data files from PDBSum Identification of Protein Pockets & Cavities at CASTp

Sequence-derived information

View one-letter amino acid or nucleotide sequence for each chain: [1mo6_A]

Other resources with information on 1MO6

InterPro: IPR003593 , IPR006141 , IPR006142 , IPR004042 , IPR001553 , IPR003587 , IPR003586 MMDB (Entrez's Structure Database)

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