Database accession: MF7000085
Name: DNA-binding protein (M. jannaschii)
PDB ID: 1ku9
Experimental method: X-ray (2.80 Å)
Assembly: Homodimer
Source organism: Methanocaldococcus jannaschii
Primary publication of the structure:
Ray SS, Bonanno JB, Chen H, de Lencastre H, Wu S, Tomasz A, Burley SK
X-ray structure of an M. jannaschii DNA-binding protein: implications for antibiotic resistance in S. aureus.
(2003) Proteins 50: 170-3
PMID: 12471609
Abstract:
Not available.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
DNA binding DNA binding
DNA-binding transcription factor activity DNA-binding transcription factor activity
Biological process: not assigned
Cellular component: not assigned
Structural annotations of the participating protein chains.Entry contents: 2 distinct polypeptide molecules
Chains: A, B
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: Putative HTH-type transcriptional regulator MJ1563
Source organism: Methanocaldococcus jannaschii
Length: 152 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMIIMEEAKKLIIELFSELAKIHGLNKSVGAVYAILYLSDKPLTISDIMEELKISKGNVSMSLKKLEELGFVRKVWIKGERKNYYEAVDGFSSIKDIAKRKHDLIAKTYEDLKKLEEKCNEEEKEFIKQKIKGIERMKKISEKILEALNDLDN
UniProtKB AC: Q58958 (positions: 1-151)
Coverage: 99%
Name: Putative HTH-type transcriptional regulator MJ1563
Source organism: Methanocaldococcus jannaschii
Length: 152 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMIIMEEAKKLIIELFSELAKIHGLNKSVGAVYAILYLSDKPLTISDIMEELKISKGNVSMSLKKLEELGFVRKVWIKGERKNYYEAVDGFSSIKDIAKRKHDLIAKTYEDLKKLEEKCNEEEKEFIKQKIKGIERMKKISEKILEALNDLDN
UniProtKB AC: Q58958 (positions: 1-151)
Coverage: 99%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: Winged helix DNA-binding domain (ArsR family) transcriptional regulator
Evidence level: Indirect evidence
Evidence coverage: Only some parts of the structure participates in mutual synergistic folding.
Complex Evidence:
The N-terminal portion of the ArsR family transcriptional regulator, Mj223, is a helix-turn-helix (HTH) winged-helix DNA-binding motif. The C-terminal region of the protein is composed of two leucine-rich α-helices (H5 and H6) that form an antiparallel four-helix bundle with a large, hydrophobic interaction surface on dimerization that forms the hydrophobic core of the dimer (PMID:12471609, PMID:9466913). The C-terminal dimerization subdomain is a nice case of MSF. The protein is a dimer in solution (Dynamic light scattering) (PMID:12471609).
Chain A:
N/A
Chain B:
N/A
Surface and contacts features:
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). Download the CIF file (.cif)
Download this entry's XML file (.xml)
Download this entry's JSON file (.json)
