Database accession: MF7000753
Name: NMB1585, a MarR family regulator (Neisseria meningitidis)
PDB ID: 3g3z
Experimental method: X-ray (2.10 Å)
Assembly: Homodimer
Source organism: Neisseria meningitidis serogroup B
Primary publication of the structure:
Nichols CE, Sainsbury S, Ren J, Walter TS, Verma A, Stammers DK, Saunders NJ, Owens RJ
The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis.
(2009) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65: 204-9
PMID: 19255465
Abstract:
The structure of the MarR-family transcription factor NMB1585 from Neisseria meningitidis has been solved using data extending to a resolution of 2.1 A. Overall, the dimeric structure resembles those of other MarR proteins, with each subunit comprising a winged helix-turn-helix (wHtH) domain connected to an alpha-helical dimerization domain. The spacing of the recognition helices of the wHtH domain indicates that NMB1585 is pre-configured for DNA binding, with a putative inducer pocket that is largely occluded by the side chains of two aromatic residues (Tyr29 and Trp53). NMB1585 was shown to bind to its own promoter region in a gel-shift assay, indicating that the protein acts as an auto-repressor.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
DNA-binding transcription factor activity DNA-binding transcription factor activity
Biological process:
regulation of DNA-templated transcription regulation of DNA-templated transcription
response to stress response to stress
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: Transcriptional regulator, MarR family
Source organism: Neisseria meningitidis serogroup B
Length: 143 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMNQLDQLGTRINLICNVFDKWIGQQDLNYNLFAVLYTLATEGSRTQKHIGEKWSLPKQTVSGVCKTLAGQGLIEWQEGEQDRRKRLLSLTETGKAYAAPLTESAQEFSDKVFATFGDKRTTRLFADLDALAEVMEKTISENKK
UniProtKB AC: Q9JYH5 (positions: 1-142)
Coverage: 99%
Name: Transcriptional regulator, MarR family
Source organism: Neisseria meningitidis serogroup B
Length: 143 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMNQLDQLGTRINLICNVFDKWIGQQDLNYNLFAVLYTLATEGSRTQKHIGEKWSLPKQTVSGVCKTLAGQGLIEWQEGEQDRRKRLLSLTETGKAYAAPLTESAQEFSDKVFATFGDKRTTRLFADLDALAEVMEKTISENKK
UniProtKB AC: Q9JYH5 (positions: 1-142)
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 (MarR type II) transcriptional regulator
Evidence level: Indirect evidence
Evidence coverage: Only some parts of the structure participates in mutual synergistic folding.
Complex Evidence:
Thermal unfolding measured with circular dichroism of the MarR family protein, HucR, suggested two-state model of unfolding (PMID:15448166). Also, a decrease in pH induced a molten globule-like state, where the protein remained in dimeric form (PMID:27282811). Helices 1, 2, 6 and 7 form the dimerization subdomain, they form an apparently stable dimer interface that preconfigures the DNA recognition HTH subdomain for DNA binding (PMID:16750221).
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)
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