This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3hyt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "3hyt" [edit=sysop:move=sysop])
Line 1: Line 1:
-
{{STRUCTURE_3hyt| PDB=3hyt | SCENE= }}
+
==Structural Basis of GDP Release and Gating in G Protein Coupled Fe2+ Transport==
-
===Structural Basis of GDP Release and Gating in G Protein Coupled Fe2+ Transport===
+
<StructureSection load='3hyt' size='340' side='right' caption='[[3hyt]], [[Resolution|resolution]] 2.74&Aring;' scene=''>
-
{{ABSTRACT_PUBMED_19629046}}
+
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[3hyt]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HYT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HYT FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGO:2-AMINO-9-(5-O-[(R)-HYDROXY{[(R)-HYDROXY(PHOSPHONOAMINO)PHOSPHORYL]OXY}PHOSPHORYL]-3-O-{[2-(METHYLAMINO)PHENYL]CARBONYL}-BETA-D-ERYTHRO-PENTOFURANOSYL-2-ULOSE)-1,9-DIHYDRO-6H-PURIN-6-ONE'>AGO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 +
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hyr|3hyr]]</td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">feoB, b3409, JW3372 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=3hyt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hyt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hyt RCSB], [http://www.ebi.ac.uk/pdbsum/3hyt PDBsum]</span></td></tr>
 +
</table>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hy/3hyt_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
G proteins are key molecular switches in the regulation of membrane protein function and signal transduction. The prokaryotic membrane protein FeoB is involved in G protein coupled Fe(2+) transport, and is unique in that the G protein is directly tethered to the membrane domain. Here, we report the structure of the soluble domain of FeoB, including the G protein domain, and its assembly into an unexpected trimer. Comparisons between nucleotide free and liganded structures reveal the closed and open state of a central cytoplasmic pore, respectively. In addition, these data provide the first observation of a conformational switch in the nucleotide-binding G5 motif, defining the structural basis for GDP release. From these results, structural parallels are drawn to eukaryotic G protein coupled membrane processes.
-
==About this Structure==
+
Structural basis of GDP release and gating in G protein coupled Fe2+ transport.,Guilfoyle A, Maher MJ, Rapp M, Clarke R, Harrop S, Jormakka M EMBO J. 2009 Sep 2;28(17):2677-85. Epub 2009 Jul 23. PMID:19629046<ref>PMID:19629046</ref>
-
[[3hyt]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HYT OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<ref group="xtra">PMID:019629046</ref><references group="xtra"/>
+
</div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Jormakka, M.]]
+
[[Category: Jormakka, M]]
-
[[Category: Maher, M J.]]
+
[[Category: Maher, M J]]
[[Category: Cell inner membrane]]
[[Category: Cell inner membrane]]
[[Category: Cell membrane]]
[[Category: Cell membrane]]

Revision as of 06:38, 18 December 2014

Structural Basis of GDP Release and Gating in G Protein Coupled Fe2+ Transport

3hyt, resolution 2.74Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3hyt"
Personal tools