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.


4r98

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:51, 1 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Chimera of the N-terminal domain of E. coli FeoB==
==Chimera of the N-terminal domain of E. coli FeoB==
-
<StructureSection load='4r98' size='340' side='right' caption='[[4r98]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
+
<StructureSection load='4r98' size='340' side='right'caption='[[4r98]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4r98]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R98 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R98 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4r98]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R98 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNH:AMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNH</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.22&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hyr|3hyr]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNH:AMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNH</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=4r98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r98 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r98 RCSB], [http://www.ebi.ac.uk/pdbsum/4r98 PDBsum]</span></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=4r98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r98 OCA], [https://pdbe.org/4r98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r98 RCSB], [https://www.ebi.ac.uk/pdbsum/4r98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r98 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/FEOB_ECOLI FEOB_ECOLI]] GTP-driven Fe(2+) uptake system.<ref>PMID:8407793</ref> <ref>PMID:12446835</ref>
+
[https://www.uniprot.org/uniprot/FEOB_ECOLI FEOB_ECOLI] GTP-driven Fe(2+) uptake system.<ref>PMID:8407793</ref> <ref>PMID:12446835</ref>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
The release of GDP from GTPases signals the initiation of a GTPase cycle, where the association of GTP triggers conformational changes promoting binding of downstream effector molecules. Studies have implicated the nucleotide-binding G5 loop to be involved in the GDP release mechanism. For example, biophysical studies on both the eukaryotic Galpha proteins and the GTPase domain (NFeoB) of prokaryotic FeoB proteins have revealed conformational changes in the G5 loop that accompany nucleotide binding and release. However, it is unclear whether this conformational change in the G5 loop is a prerequisite for GDP release, or, alternatively, the movement is a consequence of release. To gain additional insight into the sequence of events leading to GDP release, we have created a chimeric protein comprised of Escherichia coli NFeoB and the G5 loop from the human Gialpha1 protein. The protein chimera retains GTPase activity at a similar level to wild-type NFeoB, and structural analyses of the nucleotide-free and GDP-bound proteins show that the G5 loop adopts conformations analogous to that of the human nucleotide-bound Gialpha1 protein in both states. Interestingly, isothermal titration calorimetry and stopped-flow kinetic analyses reveal uncoupled nucleotide affinity and release rates, supporting a model where G5 loop movement promotes nucleotide release.
+
-
 
+
-
A GTPase chimera illustrates an uncoupled nucleotide affinity and release rate, providing insight into the activation mechanism.,Guilfoyle AP, Deshpande CN, Font Sadurni J, Ash MR, Tourle S, Schenk G, Maher MJ, Jormakka M Biophys J. 2014 Dec 16;107(12):L45-8. doi: 10.1016/j.bpj.2014.10.064. PMID:25517170<ref>PMID:25517170</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Jormakka, M]]
+
[[Category: Escherichia coli]]
-
[[Category: Maher, M J]]
+
[[Category: Large Structures]]
-
[[Category: Feob]]
+
[[Category: Jormakka M]]
-
[[Category: Metal transport]]
+
[[Category: Maher MJ]]

Current revision

Chimera of the N-terminal domain of E. coli FeoB

PDB ID 4r98

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/4r98"
Personal tools