1q1o: Difference between revisions
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==Solution Structure of the PB1 Domain of Cdc24p (Long Form)== | |||
<StructureSection load='1q1o' size='340' side='right'caption='[[1q1o]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1q1o]] 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=1Q1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q1O FirstGlance]. <br> | |||
</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=1q1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q1o OCA], [https://pdbe.org/1q1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q1o RCSB], [https://www.ebi.ac.uk/pdbsum/1q1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q1o 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. | |||
== 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/q1/1q1o_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/main_output.php?pdb_ID=1q1o ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The PC motif is evolutionarily conserved together with the PB1 domain, a binding partner of the PC motif-containing protein. For interaction with the PB1 domain, the PC motif-containing region (PCCR) comprising the PC motif and its flanking regions is required. Because the PB1 domain and the PCCR are novel binding modules found in a variety of signaling proteins, their structural and functional characterization is crucial. Bem1p and Cdc24p interact through the PB1-PCCR interaction and regulate cell polarization in budding yeast. Here, we determined a tertiary structure of the PCCR of Cdc24p by NMR. The tertiary structure of the PCCR is similar to that of the PB1 domain of Bem1p, which is classified into a ubiquitin fold. The PC motif portion takes a compact betabetaalpha-fold, presented on the ubiquitin scaffold. Mutational studies indicate that the PB1-PCCR interaction is mainly electrostatic. Based on the structural information, we group the PB1 domains and the PCCRs into a novel family, named the PB1 family. Thus, the PB1 family proteins form a specific dimer with each other. | |||
The PB1 domain and the PC motif-containing region are structurally similar protein binding modules.,Yoshinaga S, Kohjima M, Ogura K, Yokochi M, Takeya R, Ito T, Sumimoto H, Inagaki F EMBO J. 2003 Oct 1;22(19):4888-97. PMID:14517229<ref>PMID:14517229</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1q1o" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Inagaki | [[Category: Inagaki F]] | ||
[[Category: Ito | [[Category: Ito T]] | ||
[[Category: Kohjima | [[Category: Kohjima M]] | ||
[[Category: Ogura | [[Category: Ogura K]] | ||
[[Category: Sumimoto | [[Category: Sumimoto H]] | ||
[[Category: Takeya | [[Category: Takeya R]] | ||
[[Category: Yokochi | [[Category: Yokochi M]] | ||
[[Category: Yoshinaga | [[Category: Yoshinaga S]] | ||
Latest revision as of 21:15, 29 May 2024
Solution Structure of the PB1 Domain of Cdc24p (Long Form)Solution Structure of the PB1 Domain of Cdc24p (Long Form)
Structural highlights
FunctionCDC24_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 PubMedThe PC motif is evolutionarily conserved together with the PB1 domain, a binding partner of the PC motif-containing protein. For interaction with the PB1 domain, the PC motif-containing region (PCCR) comprising the PC motif and its flanking regions is required. Because the PB1 domain and the PCCR are novel binding modules found in a variety of signaling proteins, their structural and functional characterization is crucial. Bem1p and Cdc24p interact through the PB1-PCCR interaction and regulate cell polarization in budding yeast. Here, we determined a tertiary structure of the PCCR of Cdc24p by NMR. The tertiary structure of the PCCR is similar to that of the PB1 domain of Bem1p, which is classified into a ubiquitin fold. The PC motif portion takes a compact betabetaalpha-fold, presented on the ubiquitin scaffold. Mutational studies indicate that the PB1-PCCR interaction is mainly electrostatic. Based on the structural information, we group the PB1 domains and the PCCRs into a novel family, named the PB1 family. Thus, the PB1 family proteins form a specific dimer with each other. The PB1 domain and the PC motif-containing region are structurally similar protein binding modules.,Yoshinaga S, Kohjima M, Ogura K, Yokochi M, Takeya R, Ito T, Sumimoto H, Inagaki F EMBO J. 2003 Oct 1;22(19):4888-97. PMID:14517229[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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