View source for 6cah


==NMR-based structure of the FHA-2 domain from Mycobacterium tuberculosis ABC transporter Rv1747==
<StructureSection load='6cah' size='340' side='right'caption='[[6cah]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6cah]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CAH FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6cah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cah OCA], [https://pdbe.org/6cah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cah RCSB], [https://www.ebi.ac.uk/pdbsum/6cah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cah ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ABC1_MYCTU ABC1_MYCTU] Involved in the translocation of an unknown substrate across the membrane. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation. Required for virulence.<ref>PMID:15135525</ref> <ref>PMID:16040957</ref> 
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== Publication Abstract from PubMed ==
The Mycobacterium tuberculosis ATP-binding cassette transporter Rv1747 is a putative exporter of cell wall biosynthesis intermediates. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting Forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). The structures of FHA-1 and FHA-2 were determined by X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, respectively. Relative to the canonical 11-strand beta-sandwich FHA domain fold of FHA-1, FHA-2 is circularly permuted and lacking one beta-strand. Nevertheless, the two share a conserved pThr-binding cleft. FHA-2 is less stable and more dynamic than FHA-1, yet binds model pThr peptides with moderately higher affinity ( approximately 50 muM versus 500 muM equilibrium dissociation constants). Based on NMR relaxation and chemical shift perturbation measurements, when joined within a polypeptide chain, either FHA domain can bind either linker pThr to form intra- and intermolecular complexes. We hypothesize that this enables tunable phosphorylation-dependent multimerization to regulate Rv1747 transporter activity.

Biophysical Characterization of the Tandem FHA Domain Regulatory Module from the Mycobacteriumtuberculosis ABC Transporter Rv1747.,Heinkel F, Shen L, Richard-Greenblatt M, Okon M, Bui JM, Gee CL, Gay LM, Alber T, Av-Gay Y, Gsponer J, McIntosh LP Structure. 2018 May 17. pii: S0969-2126(18)30164-3. doi:, 10.1016/j.str.2018.04.018. PMID:29861345<ref>PMID:29861345</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6cah" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Gsponer J]]
[[Category: Heinkel F]]
[[Category: McIntosh LP]]
[[Category: Okon M]]