6nc4

From Proteopedia

(Difference between revisions)

Revision as of 06:53, 23 October 2019

FtsY-NG high-resolution

Structural highlights

6nc4 is a 2 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

[FTSY_ECOLI] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

The bacterial signal recognition particle (SRP) receptor, FtsY, participates with the SRP in co-translation targeting of proteins. Multiple crystal structures of the NG domain of E. coli FtsYNG have been determined at high-resolution (1.22-1.88A), in the nucleotide-free (apo) form as well as bound to GDP and non-hydrolysable GTP analogues. The combination of high-resolution and multiple solved structures of FtsYNG in different states revealed a new sensor-relay system of this unique GTPase receptor. A nucleotide sensing function of the P-loop assists FtsYNG in nucleotide-binding and contributes to modulate nucleotide binding properties in SRP GTPases. A reorganization of the other G-loops and the insertion binding domain (IBD) is observed only upon transition from a diphosphate to a triphosphate nucleotide. The role of a magnesium ion during the GDP and GTP-bound states has also been observed. The binding of magnesium in the nucleotide site causes the reorientation of the beta- and gamma- phosphate groups toward the jaws of the P-loop and stabilizes the binding of the nucleotide, creating a network of hydrogen and water-bridge interactions.

Structural insights into the G-loop dynamics of E. coli FtsY NG domain.,Faoro C, Ataide SF J Struct Biol. 2019 Sep 11. pii: S1047-8477(19)30198-4. doi:, 10.1016/j.jsb.2019.09.004. PMID:31520694^[7]

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

References

↑ Luirink J, ten Hagen-Jongman CM, van der Weijden CC, Oudega B, High S, Dobberstein B, Kusters R. An alternative protein targeting pathway in Escherichia coli: studies on the role of FtsY. EMBO J. 1994 May 15;13(10):2289-96. PMID:8194520
↑ Powers T, Walter P. Co-translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor. EMBO J. 1997 Aug 15;16(16):4880-6. PMID:9305630 doi:10.1093/emboj/16.16.4880
↑ Peluso P, Shan SO, Nock S, Herschlag D, Walter P. Role of SRP RNA in the GTPase cycles of Ffh and FtsY. Biochemistry. 2001 Dec 18;40(50):15224-33. PMID:11735405
↑ Tian H, Beckwith J. Genetic screen yields mutations in genes encoding all known components of the Escherichia coli signal recognition particle pathway. J Bacteriol. 2002 Jan;184(1):111-8. PMID:11741850
↑ Buskiewicz I, Deuerling E, Gu SQ, Jockel J, Rodnina MV, Bukau B, Wintermeyer W. Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor. Proc Natl Acad Sci U S A. 2004 May 25;101(21):7902-6. Epub 2004 May 17. PMID:15148364 doi:http://dx.doi.org/10.1073/pnas.0402231101
↑ Shan SO, Chandrasekar S, Walter P. Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation. J Cell Biol. 2007 Aug 13;178(4):611-20. Epub 2007 Aug 6. PMID:17682051 doi:http://dx.doi.org/10.1083/jcb.200702018
↑ Faoro C, Ataide SF. Structural insights into the G-loop dynamics of E. coli FtsY NG domain. J Struct Biol. 2019 Sep 11. pii: S1047-8477(19)30198-4. doi:, 10.1016/j.jsb.2019.09.004. PMID:31520694 doi:http://dx.doi.org/10.1016/j.jsb.2019.09.004

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/6nc4"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6nc4 is ON HOLD  until Paper Publication
+==FtsY-NG high-resolution==
+<StructureSection load='6nc4' size='340' side='right'caption='[[6nc4]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6nc4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NC4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NC4 FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</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=6nc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nc4 OCA], [http://pdbe.org/6nc4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nc4 RCSB], [http://www.ebi.ac.uk/pdbsum/6nc4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nc4 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/FTSY_ECOLI FTSY_ECOLI]] Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components.<ref>PMID:8194520</ref> <ref>PMID:9305630</ref> <ref>PMID:11735405</ref> <ref>PMID:11741850</ref> <ref>PMID:15148364</ref> <ref>PMID:17682051</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The bacterial signal recognition particle (SRP) receptor, FtsY, participates with the SRP in co-translation targeting of proteins. Multiple crystal structures of the NG domain of E. coli FtsYNG have been determined at high-resolution (1.22-1.88A), in the nucleotide-free (apo) form as well as bound to GDP and non-hydrolysable GTP analogues. The combination of high-resolution and multiple solved structures of FtsYNG in different states revealed a new sensor-relay system of this unique GTPase receptor. A nucleotide sensing function of the P-loop assists FtsYNG in nucleotide-binding and contributes to modulate nucleotide binding properties in SRP GTPases. A reorganization of the other G-loops and the insertion binding domain (IBD) is observed only upon transition from a diphosphate to a triphosphate nucleotide. The role of a magnesium ion during the GDP and GTP-bound states has also been observed. The binding of magnesium in the nucleotide site causes the reorientation of the beta- and gamma- phosphate groups toward the jaws of the P-loop and stabilizes the binding of the nucleotide, creating a network of hydrogen and water-bridge interactions.
-Authors: Ataide, S.F., Faoro, C.
+Structural insights into the G-loop dynamics of E. coli FtsY NG domain.,Faoro C, Ataide SF J Struct Biol. 2019 Sep 11. pii: S1047-8477(19)30198-4. doi:, 10.1016/j.jsb.2019.09.004. PMID:31520694<ref>PMID:31520694</ref>
-Description: FtsY-NG high-resolution
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Ataide, S.F]]
+<div class="pdbe-citations 6nc4" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Ataide, S F]]
 [[Category: Faoro, C]]
+[[Category: Ftsy]]
+[[Category: Signal recognition particle receptor]]
+[[Category: Sr]]
+[[Category: Srp]]
+[[Category: Transport protein]]

6nc4

From Proteopedia

Revision as of 06:53, 23 October 2019

FtsY-NG high-resolution

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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