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.

7m3p

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Xrcc4-Spc110p(164-207) fusion

Structural highlights

7m3p is a 2 chain structure with sequence from Homo sapiens and Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.0000186Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

XRCC4_HUMAN Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.^[1] ^[2] ^[3] ^[4] SP110_YEAST Component of the spindle pole body (SPB) required for the proper execution of spindle pole body (SPB) duplication. Potential role in cross-linking filaments or anchoring other molecules. It is essential for growth.^[5] ^[6] ^[7] ^[8] ^[9] ^[10]

Publication Abstract from PubMed

Microtubule (MT) nucleation is regulated by the gamma-tubulin ring complex (gammaTuRC), conserved from yeast to humans. In Saccharomyces cerevisiae, gammaTuRC is composed of seven identical gamma-tubulin small complex (gammaTuSC) sub-assemblies, which associate helically to template MT growth. gammaTuRC assembly provides a key point of regulation for the MT cytoskeleton. Here, we combine crosslinking mass spectrometry, X-ray crystallography, and cryo-EM structures of both monomeric and dimeric gammaTuSCs, and open and closed helical gammaTuRC assemblies in complex with Spc110p to elucidate the mechanisms of gammaTuRC assembly. gammaTuRC assembly is substantially aided by the evolutionarily conserved CM1 motif in Spc110p spanning a pair of adjacent gammaTuSCs. By providing the highest resolution and most complete views of any gammaTuSC assembly, our structures allow phosphorylation sites to be mapped, surprisingly suggesting that they are mostly inhibitory. A comparison of our structures with the CM1 binding site in the human gammaTuRC structure at the interface between GCP2 and GCP6 allows for the interpretation of significant structural changes arising from CM1 helix binding to metazoan gammaTuRC.

CM1-driven assembly and activation of yeast gamma-tubulin small complex underlies microtubule nucleation.,Brilot AF, Lyon AS, Zelter A, Viswanath S, Maxwell A, MacCoss MJ, Muller EG, Sali A, Davis TN, Agard DA Elife. 2021 May 5;10. pii: 65168. doi: 10.7554/eLife.65168. PMID:33949948^[11]

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

References

↑ Li Z, Otevrel T, Gao Y, Cheng HL, Seed B, Stamato TD, Taccioli GE, Alt FW. The XRCC4 gene encodes a novel protein involved in DNA double-strand break repair and V(D)J recombination. Cell. 1995 Dec 29;83(7):1079-89. PMID:8548796
↑ Chen L, Trujillo K, Sung P, Tomkinson AE. Interactions of the DNA ligase IV-XRCC4 complex with DNA ends and the DNA-dependent protein kinase. J Biol Chem. 2000 Aug 25;275(34):26196-205. PMID:10854421 doi:10.1074/jbc.M000491200
↑ Nick McElhinny SA, Snowden CM, McCarville J, Ramsden DA. Ku recruits the XRCC4-ligase IV complex to DNA ends. Mol Cell Biol. 2000 May;20(9):2996-3003. PMID:10757784
↑ Foster RE, Nnakwe C, Woo L, Frank KM. Monoubiquitination of the nonhomologous end joining protein XRCC4. Biochem Biophys Res Commun. 2006 Mar 3;341(1):175-83. Epub 2006 Jan 6. PMID:16412978 doi:S0006-291X(05)02903-7
↑ Elliott S, Knop M, Schlenstedt G, Schiebel E. Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication. Proc Natl Acad Sci U S A. 1999 May 25;96(11):6205-10. PMID:10339566
↑ Friedman DB, Kern JW, Huneycutt BJ, Vinh DB, Crawford DK, Steiner E, Scheiltz D, Yates J 3rd, Resing KA, Ahn NG, Winey M, Davis TN. Yeast Mps1p phosphorylates the spindle pole component Spc110p in the N-terminal domain. J Biol Chem. 2001 May 25;276(21):17958-67. Epub 2001 Mar 6. PMID:11278681 doi:http://dx.doi.org/10.1074/jbc.M010461200
↑ Mirzayan C, Copeland CS, Snyder M. The NUF1 gene encodes an essential coiled-coil related protein that is a potential component of the yeast nucleoskeleton. J Cell Biol. 1992 Mar;116(6):1319-32. PMID:1541631
↑ Huisman SM, Smeets MF, Segal M. Phosphorylation of Spc110p by Cdc28p-Clb5p kinase contributes to correct spindle morphogenesis in S. cerevisiae. J Cell Sci. 2007 Feb 1;120(Pt 3):435-46. Epub 2007 Jan 9. PMID:17213332 doi:http://dx.doi.org/10.1242/jcs.03342
↑ Kilmartin JV, Dyos SL, Kershaw D, Finch JT. A spacer protein in the Saccharomyces cerevisiae spindle poly body whose transcript is cell cycle-regulated. J Cell Biol. 1993 Dec;123(5):1175-84. PMID:7503995
↑ Knop M, Schiebel E. Spc98p and Spc97p of the yeast gamma-tubulin complex mediate binding to the spindle pole body via their interaction with Spc110p. EMBO J. 1997 Dec 1;16(23):6985-95. PMID:9384578 doi:http://dx.doi.org/10.1093/emboj/16.23.6985
↑ Brilot AF, Lyon AS, Zelter A, Viswanath S, Maxwell A, MacCoss MJ, Muller EG, Sali A, Davis TN, Agard DA. CM1-driven assembly and activation of yeast gamma-tubulin small complex underlies microtubule nucleation. Elife. 2021 May 5;10. pii: 65168. doi: 10.7554/eLife.65168. PMID:33949948 doi:http://dx.doi.org/10.7554/eLife.65168

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/7m3p"

@@ Line 3: / Line 3: @@
 <StructureSection load='7m3p' size='340' side='right'caption='[[7m3p]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[7m3p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7M3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M3P FirstGlance]. <br>
+<table><tr><td colspan='2'>[[7m3p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7M3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7M3P FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SCNYR20_0001052900, SCP684_0001052400 ([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">X-ray diffraction, [[Resolution|Resolution]] 2.0000186&#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=7m3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7m3p OCA], [https://pdbe.org/7m3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7m3p RCSB], [https://www.ebi.ac.uk/pdbsum/7m3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7m3p ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/XRCC4_HUMAN XRCC4_HUMAN]] Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.<ref>PMID:8548796</ref> <ref>PMID:10854421</ref> <ref>PMID:10757784</ref> <ref>PMID:16412978</ref>
+[https://www.uniprot.org/uniprot/XRCC4_HUMAN XRCC4_HUMAN] Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex is responsible for the NHEJ ligation step, and XRCC4 enhances the joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends.<ref>PMID:8548796</ref> <ref>PMID:10854421</ref> <ref>PMID:10757784</ref> <ref>PMID:16412978</ref> [https://www.uniprot.org/uniprot/SP110_YEAST SP110_YEAST] Component of the spindle pole body (SPB) required for the proper execution of spindle pole body (SPB) duplication. Potential role in cross-linking filaments or anchoring other molecules. It is essential for growth.<ref>PMID:10339566</ref> <ref>PMID:11278681</ref> <ref>PMID:1541631</ref> <ref>PMID:17213332</ref> <ref>PMID:7503995</ref> <ref>PMID:9384578</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Agard, D A]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Brilot, A F]]
+[[Category: Agard DA]]
-[[Category: Davis, T N]]
+[[Category: Brilot AF]]
-[[Category: Lyon, A S]]
+[[Category: Davis TN]]
-[[Category: MacCoss, M J]]
+[[Category: Lyon AS]]
-[[Category: Maxwell, A]]
+[[Category: MacCoss MJ]]
-[[Category: Muller, E G]]
+[[Category: Maxwell A]]
-[[Category: Sali, A]]
+[[Category: Muller EG]]
-[[Category: Viswanath, S]]
+[[Category: Sali A]]
-[[Category: Zelter, A]]
+[[Category: Viswanath S]]
-[[Category: Cell cycle]]
+[[Category: Zelter A]]
-[[Category: Microtubule nucleation]]

7m3p

From Proteopedia

Current revision

Xrcc4-Spc110p(164-207) fusion

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox