 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transcription
|
PDB id
|
|
|
|
3g3z
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Transcription
|
|
|
Title:
|
|
The structure of nmb1585, a marr family regulator from neiss meningitidis
|
|
Structure:
|
|
Transcriptional regulator, marr family. Chain: a, b. Synonym: nmb1585. Engineered: yes
|
|
Source:
|
|
Neisseria meningitidis serogroup b. Organism_taxid: 491. Strain: mc58. Gene: nmb1585. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
Resolution:
|
|
|
2.10Å
|
R-factor:
|
0.206
|
R-free:
|
0.266
|
|
|
Authors:
|
|
C.E.Nichols,S.Sainsbury,J.Ren,T.S.Walter,A.Verma,D.K.Stammer N.J.Saunders,R.J.Owens,Oxford Protein Production Facility (
|
|
Key ref:
|
|
C.E.Nichols
et al.
(2009).
The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis.
Acta Crystallogr Sect F Struct Biol Cryst Commun,
65,
204-209.
PubMed id:
Ref:
|
|
|
Date:
|
|
|
03-Feb-09
|
Release date:
|
14-Apr-09
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
Q9JYH5
(Q9JYH5_NEIMB) -
Transcriptional regulator, MarR family
|
|
|
|
Seq:
Struc:
|
|
|
|
143 a.a.
142 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
 |
PfamA domain |
|
|
 |
Secondary structure |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Gene Ontology (GO) functional annotation
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Cellular component
|
intracellular
|
1 term
|
|
|
Biological process
|
transcription, DNA-dependent
|
2 terms
|
|
|
Biochemical function
|
DNA binding
|
2 terms
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
Acta Crystallogr Sect F Struct Biol Cryst Commun
65:204-209
(2009)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis.
|
|
C.E.Nichols,
S.Sainsbury,
J.Ren,
T.S.Walter,
A.Verma,
D.K.Stammers,
N.J.Saunders,
R.J.Owens.
|
|
|
|
|
| |
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.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Links
