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.

1xko

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Structure of Thermotoga maritima CheX

Structural highlights

1xko is a 2 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.48Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CHEX_THEMA Involved in restoring normal CheY-P levels by dephosphorylating CheY-P. It has a greater activity than CheC.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

In bacterial chemotaxis, phosphorylated CheY levels control the sense of flagella rotation and thereby determine swimming behavior. In E. coli, CheY dephosphorylation by CheZ extinguishes the switching signal. But, instead of CheZ, many chemotactic bacteria contain CheC, CheD, and/or CheX. The crystal structures of T. maritima CheC and CheX reveal a common fold unlike that of any other known protein. Unlike CheC, CheX dimerizes via a continuous beta sheet between subunits. T. maritima CheC, as well as CheX, dephosphorylate CheY, although CheC requires binding of CheD to achieve the activity of CheX. Structural analyses identified one conserved active site in CheX and two in CheC; mutations therein reduce CheY-phosphatase activity, but only mutants of two invariant asparagine residues are completely inactive even in the presence of CheD. Our structures indicate that the flagellar switch components FliY and FliM resemble CheC more closely than CheX, but attribute phosphatase activity only to FliY.

Structure and function of an unusual family of protein phosphatases: the bacterial chemotaxis proteins CheC and CheX.,Park SY, Chao X, Gonzalez-Bonet G, Beel BD, Bilwes AM, Crane BR Mol Cell. 2004 Nov 19;16(4):563-74. PMID:15546616^[1]

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

References

↑ Park SY, Chao X, Gonzalez-Bonet G, Beel BD, Bilwes AM, Crane BR. Structure and function of an unusual family of protein phosphatases: the bacterial chemotaxis proteins CheC and CheX. Mol Cell. 2004 Nov 19;16(4):563-74. PMID:15546616 doi:http://dx.doi.org/10.1016/j.molcel.2004.10.018

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1xko"

@@ Line 3: / Line 3: @@
 <StructureSection load='1xko' size='340' side='right'caption='[[1xko]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1xko]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XKO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1xko]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XKO FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1squ|1squ]]</div></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]] 2.48&#8491;</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=1xko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xko OCA], [https://pdbe.org/1xko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xko RCSB], [https://www.ebi.ac.uk/pdbsum/1xko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xko ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/CHEX_THEMA CHEX_THEMA] Involved in restoring normal CheY-P levels by dephosphorylating CheY-P. It has a greater activity than CheC.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 43589]]
 [[Category: Large Structures]]
-[[Category: Beel, B D]]
+[[Category: Thermotoga maritima]]
-[[Category: Bilwes, A M]]
+[[Category: Beel BD]]
-[[Category: Chao, X]]
+[[Category: Bilwes AM]]
-[[Category: Crane, B R]]
+[[Category: Chao X]]
-[[Category: Gonzalez-Bonet, G]]
+[[Category: Crane BR]]
-[[Category: Park, S Y]]
+[[Category: Gonzalez-Bonet G]]
-[[Category: Attractant]]
+[[Category: Park SY]]
-[[Category: Chemotaxis]]
-[[Category: Protein phosphatase]]
-[[Category: Signal transduction]]

1xko

From Proteopedia

Current revision

Structure of Thermotoga maritima CheX

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox