6ccd

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(Difference between revisions)

Revision as of 05:50, 20 June 2018

The crystal structure of Mycobacterium tuberculosis Rv1747 FHA-1

Structural highlights

6ccd is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
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/6ccd"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6ccd is ON HOLD  until Paper Publication
+==The crystal structure of Mycobacterium tuberculosis Rv1747 FHA-1==
+<StructureSection load='6ccd' size='340' side='right' caption='[[6ccd]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6ccd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CCD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CCD FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6ccd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ccd OCA], [http://pdbe.org/6ccd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ccd RCSB], [http://www.ebi.ac.uk/pdbsum/6ccd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ccd ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://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>
+<div style="background-color:#fffaf0;">
+== 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.
-Authors: Gay, L.M., Gee, C.L., Alber, T.
+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>
-Description: The crystal structure of Mycobacterium tuberculosis Rv1747 FHA-1
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Gee, C.L]]
+<div class="pdbe-citations 6ccd" style="background-color:#fffaf0;"></div>
-[[Category: Gay, L.M]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Alber, T]]
+[[Category: Gay, L M]]
+[[Category: Gee, C L]]
+[[Category: Fha domain]]
+[[Category: Phospho-peptide binding domain]]
+[[Category: Phospho-threonine binding domain]]
+[[Category: Protein binding]]

6ccd

From Proteopedia

Revision as of 05:50, 20 June 2018

The crystal structure of Mycobacterium tuberculosis Rv1747 FHA-1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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