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3zn3

From Proteopedia

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Current revision

N-terminal domain of S. pombe Cdc23 APC subunit

Structural highlights

3zn3 is a 1 chain structure with sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

APC8_SCHPO Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. Has a role in promoting metaphase to anaphase transition via the ubiquitination of specific mitotic substrates.^[1]

Publication Abstract from PubMed

The anaphase-promoting complex or cyclosome (APC/C) is a large E3 RING-cullin ubiquitin ligase composed of between 14 and 15 individual proteins. A striking feature of the APC/C is that only four proteins are involved in directly recognizing target proteins and catalyzing the assembly of a polyubiquitin chain. All other subunits, which account for >80% of the mass of the APC/C, provide scaffolding functions. A major proportion of these scaffolding subunits are structurally related. In metazoans, there are four canonical tetratricopeptide repeat (TPR) proteins that form homo-dimers (Apc3/Cdc27, Apc6/Cdc16, Apc7 and Apc8/Cdc23). Here, we describe the crystal structure of the N-terminal homo-dimerization domain of Schizosaccharomyces pombe Cdc23 (Cdc23Nterm). Cdc23Nterm is composed of seven contiguous TPR motifs that self-associate through a related mechanism to those of Cdc16 and Cdc27. Using the Cdc23Nterm structure, we generated a model of full-length Cdc23. The resultant "V"-shaped molecule docks into the Cdc23-assigned density of the human APC/C structure determined using negative stain electron microscopy (EM). Based on sequence conservation, we propose that Apc7 forms a homo-dimeric structure equivalent to those of Cdc16, Cdc23 and Cdc27. The model is consistent with the Apc7-assigned density of the human APC/C EM structure. The four canonical homo-dimeric TPR proteins of human APC/C stack in parallel on one side of the complex. Remarkably, the uniform relative packing of neighboring TPR proteins generates a novel left-handed suprahelical TPR assembly. This finding has implications for understanding the assembly of other TPR-containing multimeric complexes.

The Four Canonical TPR Subunits of Human APC/C Form Related Homo-Dimeric Structures and Stack in Parallel to Form a TPR Suprahelix.,Zhang Z, Chang L, Yang J, Conin N, Kulkarni K, Barford D J Mol Biol. 2013 Apr 11. pii: S0022-2836(13)00233-7. doi:, 10.1016/j.jmb.2013.04.004. PMID:23583778^[2]

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

References

↑ Yamashita YM, Nakaseko Y, Kumada K, Nakagawa T, Yanagida M. Fission yeast APC/cyclosome subunits, Cut20/Apc4 and Cut23/Apc8, in regulating metaphase-anaphase progression and cellular stress responses. Genes Cells. 1999 Aug;4(8):445-63. PMID:10526233
↑ Zhang Z, Chang L, Yang J, Conin N, Kulkarni K, Barford D. The Four Canonical TPR Subunits of Human APC/C Form Related Homo-Dimeric Structures and Stack in Parallel to Form a TPR Suprahelix. J Mol Biol. 2013 Apr 11. pii: S0022-2836(13)00233-7. doi:, 10.1016/j.jmb.2013.04.004. PMID:23583778 doi:http://dx.doi.org/10.1016/j.jmb.2013.04.004

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3zn3"

@@ Line 3: / Line 3: @@
 <StructureSection load='3zn3' size='340' side='right'caption='[[3zn3]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3zn3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZN3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZN3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3zn3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZN3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZN3 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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]] 1.9&#8491;</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=3zn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zn3 OCA], [http://pdbe.org/3zn3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zn3 RCSB], [http://www.ebi.ac.uk/pdbsum/3zn3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zn3 ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></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=3zn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zn3 OCA], [https://pdbe.org/3zn3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zn3 RCSB], [https://www.ebi.ac.uk/pdbsum/3zn3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zn3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/APC8_SCHPO APC8_SCHPO]] Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. Has a role in promoting metaphase to anaphase transition via the ubiquitination of specific mitotic substrates.<ref>PMID:10526233</ref>
+[https://www.uniprot.org/uniprot/APC8_SCHPO APC8_SCHPO] Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. Has a role in promoting metaphase to anaphase transition via the ubiquitination of specific mitotic substrates.<ref>PMID:10526233</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Cbs 356]]
 [[Category: Large Structures]]
-[[Category: Barford, D]]
+[[Category: Schizosaccharomyces pombe]]
-[[Category: Conin, N]]
+[[Category: Barford D]]
-[[Category: Kulkarni, K]]
+[[Category: Conin N]]
-[[Category: Yang, J]]
+[[Category: Kulkarni K]]
-[[Category: Zhang, Z]]
+[[Category: Yang J]]
-[[Category: Cell cycle]]
+[[Category: Zhang Z]]
-[[Category: Tpr]]

3zn3

From Proteopedia

Current revision

N-terminal domain of S. pombe Cdc23 APC subunit

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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