PDBsum entry 2zrh

Go to PDB code: 
protein ligands links
Hydrolase PDB id
Jmol PyMol
Protein chain
319 a.a. *
Waters ×24
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Msreca q196a form iv
Structure: Protein reca. Chain: a. Synonym: recombinase a. Engineered: yes. Mutation: yes
Source: Mycobacterium smegmatis str. Mc2 155. Organism_taxid: 246196. Expressed in: escherichia coli. Expression_system_taxid: 562.
3.20Å     R-factor:   0.195     R-free:   0.253
Authors: J.R.Prabu,G.P.Manjunath,N.R.Chandra,K.Muniyappa,M.Vijayan
Key ref:
J.R.Prabu et al. (2008). Functionally important movements in RecA molecules and filaments: studies involving mutation and environmental changes. Acta Crystallogr D Biol Crystallogr, 64, 1146-1157. PubMed id: 19020353 DOI: 10.1107/S0907444908028448
27-Aug-08     Release date:   09-Dec-08    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q59560  (RECA_MYCS2) -  Protein RecA
349 a.a.
319 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.  - Deleted entry.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     response to DNA damage stimulus   4 terms 
  Biochemical function     nucleotide binding     4 terms  


DOI no: 10.1107/S0907444908028448 Acta Crystallogr D Biol Crystallogr 64:1146-1157 (2008)
PubMed id: 19020353  
Functionally important movements in RecA molecules and filaments: studies involving mutation and environmental changes.
J.R.Prabu, G.P.Manjunath, N.R.Chandra, K.Muniyappa, M.Vijayan.
The crystal structures of mutants of Mycobacterium smegmatis RecA (MsRecA) involving changes of Gln196 from glutamine to alanine, asparagine and glutamic acid, wild-type MsRecA and several of their nucleotide complexes have been determined using mostly low-temperature and partly room-temperature X-ray data. At both temperatures, nucleotide binding results in a movement of Gln196 towards the bound nucleotide in the wild-type protein. This movement is abolished in the mutants, thus establishing the structural basis for the triggering action of the residue in terms of the size, shape and the chemical nature of the side chain. The 19 crystal structures reported here, together with 11 previously reported MsRecA structures, provide further elaboration of the relation between the pitch of the ;inactive' RecA filament, the orientation of the C-terminal domain with respect to the main domain and the location of the switch residue. The low-temperature structures define one extreme of the range of positions the C-terminal domain can occupy. The movement of the C-terminal domain is correlated with those of the LexA-binding loop and the loop that connects the main and the N-terminal domains. These elements of molecular plasticity are made use of in the transition to the ;active' filament, as evidenced by the recently reported structures of RecA-DNA complexes. The available structures of RecA resulting from X-ray and electron-microscopic studies appear to represent different stages in the trajectory of the allosteric transformations of the RecA filament. The work reported here contributes to the description of the early stages of this trajectory and provides insight into structures relevant to the later stages.
  Selected figure(s)  
Figure 3.
Figure 3 Snapshots in the trajectory of transformation from form I to form IV. See text for details.
Figure 7.
Figure 7 The position of the N-domain with respect to the rest of the molecule in `inactive' (green) and `active' (magenta) filaments.
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2008, 64, 1146-1157) copyright 2008.  
  Figures were selected by an automated process.