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1pqs

From Proteopedia

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Current revision

Solution structure of the C-terminal OPCA domain of yCdc24p

Structural highlights

1pqs is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CDC24_YEAST Promotes the exchange of CDC42-bound GDP by GTP. Controls the polarity of calmodulin, and the calcium regulatory process of bud emergence. CDC24 may be involved in the initial selection and organization of the budding site.

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

Phox and Bem1 (PB1) domains mediate protein-protein interactions via the formation of homo- or hetero-dimers. The C-terminal PB1 domain of yeast cell division cycle 24 (CDC24p), a guanine-nucleotide exchange factor involved in cell polarity establishment, is known to interact with the PB1 domain occurring in bud emergence MSB1 interacting 1 (BEM1p) during the regulation of the yeast budding process via its OPR/PC/AID (OPCA) motif. Here, we present the structure of an N-terminally truncated version of the Sc CDC24p PB1 domain. It shows a different topology of the beta-sheet than the long form. However, the C-terminal part of the structure shows the conserved PB1 domain features including the OPCA motif with a slight rearrangement of helix alpha1. Residues which are important for the heterodimerization with BEM1p are structurally preserved.

The solution structure of an N-terminally truncated version of the yeast CDC24p PB1 domain shows a different beta-sheet topology.,Leitner D, Wahl M, Labudde D, Krause G, Diehl A, Schmieder P, Pires JR, Fossi M, Wiedemann U, Leidert M, Oschkinat H FEBS Lett. 2005 Jul 4;579(17):3534-8. PMID:15961083^[1]

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

References

↑ Leitner D, Wahl M, Labudde D, Krause G, Diehl A, Schmieder P, Pires JR, Fossi M, Wiedemann U, Leidert M, Oschkinat H. The solution structure of an N-terminally truncated version of the yeast CDC24p PB1 domain shows a different beta-sheet topology. FEBS Lett. 2005 Jul 4;579(17):3534-8. PMID:15961083 doi:10.1016/j.febslet.2005.05.025

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Solution structure of the C-terminal OPCA domain of yCdc24p==
-<StructureSection load='1pqs' size='340' side='right'caption='[[1pqs]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1pqs' size='340' side='right'caption='[[1pqs]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1pqs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PQS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1pqs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PQS FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cdc24p ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1pqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pqs OCA], [https://pdbe.org/1pqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pqs RCSB], [https://www.ebi.ac.uk/pdbsum/1pqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pqs ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CDC24_YEAST CDC24_YEAST]] Promotes the exchange of CDC42-bound GDP by GTP. Controls the polarity of calmodulin, and the calcium regulatory process of bud emergence. CDC24 may be involved in the initial selection and organization of the budding site.
+[https://www.uniprot.org/uniprot/CDC24_YEAST CDC24_YEAST] Promotes the exchange of CDC42-bound GDP by GTP. Controls the polarity of calmodulin, and the calcium regulatory process of bud emergence. CDC24 may be involved in the initial selection and organization of the budding site.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
 [[Category: Large Structures]]
-[[Category: Diehl, A]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Fossi, M]]
+[[Category: Diehl A]]
-[[Category: Krause, G]]
+[[Category: Fossi M]]
-[[Category: Labudde, D]]
+[[Category: Krause G]]
-[[Category: Leidert, M]]
+[[Category: Labudde D]]
-[[Category: Leitner, D]]
+[[Category: Leidert M]]
-[[Category: Oschkinat, H]]
+[[Category: Leitner D]]
-[[Category: Pires, J R]]
+[[Category: Oschkinat H]]
-[[Category: Schmieder, P]]
+[[Category: Pires JR]]
-[[Category: Wahl, M]]
+[[Category: Schmieder P]]
-[[Category: Alpha and beta protein]]
+[[Category: Wahl M]]
-[[Category: Cell cycle]]

1pqs

From Proteopedia

Current revision

Solution structure of the C-terminal OPCA domain of yCdc24p

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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