4ndw

Crystal STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ESX-1 SECRETED PROTEIN REGULATOR (EspR)

spinqualitylabelsall models 4ndw, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ndw is a 2 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3qf3, 3r1f Gene: espR, MT3964, Rv3849, RV3849C ("Bacillus tuberculosis" (Zopf 1883) Klein 1884) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ESPR_MYCTU] Virulence regulator that has both architectural and regulatory roles. Impacts cell wall functions and pathogenesis through regulation of multiple genes, including the espACD operon, which is a key ESX-1 component. Influences target gene expression positively or negatively, depending on its binding position relative to the genes it controls. Acts by binding directly to the DNA. May play a central role in regulating virulence gene expression. Publication Abstract from PubMed The Mycobacterium tuberculosis ESX-1 secreted protein regulator (EspR, Rv3849) is the key protein that delivers bacterial proteins into the host cell during mycobacterial infection. EspR binds directly to the espACD operon and is involved in transcriptional activation. In the current study, M. tuberculosis EspR has been crystallized and its X-ray structure has been determined at 3.3 A resolution in a P3221 crystal form. EspR forms a physiological dimer in the crystal. Each EspR monomer contains an N-terminal helix-turn-helix DNA-binding domain and a C-terminal dimerization domain. The EspR structure in the P3221 crystal form was compared with previously determined EspR structures in P32, P21 and P212121 crystal forms. Structural comparison analysis indicated that the N-terminal helix-turn-helix domain of EspR acquires a rigid structure in the four crystal forms. However, significant structural differences were observed in the C-terminal domain of EspR in the P21 crystal form when compared with the P3221 and P32 crystal forms. The interaction, stabilization energy and buried surface area analysis of EspR in the four different crystal forms have provided information about the physiological dimer interface of EspR. Comparison of four different crystal forms of the Mycobacterium tuberculosis ESX-1 secreted protein regulator EspR.,Gangwar SP, Meena SR, Saxena AK Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):433-7. doi:, 10.1107/S2053230X14004166. Epub 2014 Mar 25. PMID:24699733 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA