6cah

From Proteopedia

(Difference between revisions)

Revision as of 09:44, 18 July 2018

NMR-based structure of the FHA-2 domain from Mycobacterium tuberculosis ABC transporter Rv1747

Structural highlights

6cah is a 1 chain structure with sequence from Myctu. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	Rv1747 (MYCTU)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Molle V, Soulat D, Jault JM, Grangeasse C, Cozzone AJ, Prost JF. Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis. FEMS Microbiol Lett. 2004 May 15;234(2):215-23. doi:, 10.1016/j.femsle.2004.03.033. PMID:15135525 doi:http://dx.doi.org/10.1016/j.femsle.2004.03.033
↑ Curry JM, Whalan R, Hunt DM, Gohil K, Strom M, Rickman L, Colston MJ, Smerdon SJ, Buxton RS. An ABC transporter containing a forkhead-associated domain interacts with a serine-threonine protein kinase and is required for growth of Mycobacterium tuberculosis in mice. Infect Immun. 2005 Aug;73(8):4471-7. doi: 10.1128/IAI.73.8.4471-4477.2005. PMID:16040957 doi:http://dx.doi.org/10.1128/IAI.73.8.4471-4477.2005
↑ Heinkel F, Shen L, Richard-Greenblatt M, Okon M, Bui JM, Gee CL, Gay LM, Alber T, Av-Gay Y, Gsponer J, McIntosh LP. Biophysical Characterization of the Tandem FHA Domain Regulatory Module from the Mycobacteriumtuberculosis ABC Transporter Rv1747. Structure. 2018 May 17. pii: S0969-2126(18)30164-3. doi:, 10.1016/j.str.2018.04.018. PMID:29861345 doi:http://dx.doi.org/10.1016/j.str.2018.04.018

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6cah"

@@ Line 3: / Line 3: @@
 <StructureSection load='6cah' size='340' side='right' caption='[[6cah]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6cah]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CAH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6cah]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. 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 [http://oca.weizmann.ac.il/oca-docs/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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6cah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cah OCA], [http://pdbe.org/6cah PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cah RCSB], [http://www.ebi.ac.uk/pdbsum/6cah PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cah ProSAT]</span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv1747 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6cah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cah OCA], [http://pdbe.org/6cah PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cah RCSB], [http://www.ebi.ac.uk/pdbsum/6cah PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cah ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Myctu]]
 [[Category: Gsponer, J]]
 [[Category: Heinkel, F]]

6cah

From Proteopedia

Revision as of 09:44, 18 July 2018

NMR-based structure of the FHA-2 domain from Mycobacterium tuberculosis ABC transporter Rv1747

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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