Structural highlights
4kbm 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.
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| Related: | 4kbj |
| Gene: | MT0695, MTCI376.08c, rpoB, Rv0667 ("Bacillus tuberculosis" (Zopf 1883) Klein 1884), carD, MT3689, Rv3583c ("Bacillus tuberculosis" (Zopf 1883) Klein 1884) |
| Activity: | DNA-directed RNA polymerase, with EC number 2.7.7.6 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[RPOB_MYCTU] DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01321] [CARD_MYCTU] Controls rRNA transcription by binding to the RNA polymerase (RNAP). Required for replication and persistence during infection of mice.[1] [2]
Publication Abstract from PubMed
CarD from Mycobacterium tuberculosis (Mtb) is an essential protein shown to be involved in stringent response through downregulation of rRNA and ribosomal protein genes. CarD interacts with the beta-subunit of RNAP and this interaction is vital for Mtb's survival during the persistent infection state. We have determined the crystal structure of CarD in complex with the RNAP beta-subunit beta1 and beta2 domains at 2.1 A resolution. The structure reveals the molecular basis of CarD/RNAP interaction, providing a basis to further our understanding of RNAP regulation by CarD. The structural fold of the CarD N-terminal domain is conserved in RNAP interacting proteins such as TRCF-RID and CdnL, and displays similar interactions to the predicted homology model based on the TRCF/RNAP beta1 structure. Interestingly, the structure of the C-terminal domain, which is required for complete CarD function in vivo, represents a distinct DNA-binding fold.
Structure of the Mtb CarD/RNAP beta-Lobes Complex Reveals the Molecular Basis of Interaction and Presents a Distinct DNA-Binding Domain for Mtb CarD.,Gulten G, Sacchettini JC Structure. 2013 Sep 17. pii: S0969-2126(13)00306-7. doi:, 10.1016/j.str.2013.08.014. PMID:24055315[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Stallings CL, Stephanou NC, Chu L, Hochschild A, Nickels BE, Glickman MS. CarD is an essential regulator of rRNA transcription required for Mycobacterium tuberculosis persistence. Cell. 2009 Jul 10;138(1):146-59. doi: 10.1016/j.cell.2009.04.041. PMID:19596241 doi:10.1016/j.cell.2009.04.041
- ↑ Weiss LA, Harrison PG, Nickels BE, Glickman MS, Campbell EA, Darst SA, Stallings CL. Interaction of CarD with RNA polymerase mediates Mycobacterium tuberculosis viability, rifampin resistance, and pathogenesis. J Bacteriol. 2012 Oct;194(20):5621-31. Epub 2012 Aug 17. PMID:22904282 doi:10.1128/JB.00879-12
- ↑ Gulten G, Sacchettini JC. Structure of the Mtb CarD/RNAP beta-Lobes Complex Reveals the Molecular Basis of Interaction and Presents a Distinct DNA-Binding Domain for Mtb CarD. Structure. 2013 Sep 17. pii: S0969-2126(13)00306-7. doi:, 10.1016/j.str.2013.08.014. PMID:24055315 doi:http://dx.doi.org/10.1016/j.str.2013.08.014
