8usp: Difference between revisions

Latest revision as of 23:16, 27 December 2023

Structural and biochemical investigations of a HEAT-repeat protein involved in the cytosolic iron-sulfur cluster assembly pathway

Structural highlights

8usp is a 6 chain structure with sequence from Saccharomyces. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MET18_YEAST Key component of the cytosolic iron-sulfur protein assembly (CIA) machinery that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. Acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as RAD3/XPD and DNA2, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription.^[1] ^[2] ^[3] ^[4] ^[5]

References

↑ Kou H, Zhou Y, Gorospe RM, Wang Z. Mms19 protein functions in nucleotide excision repair by sustaining an adequate cellular concentration of the TFIIH component Rad3. Proc Natl Acad Sci U S A. 2008 Oct 14;105(41):15714-9. PMID:18836076 doi:10.1073/pnas.0710736105
↑ Stehling O, Vashisht AA, Mascarenhas J, Jonsson ZO, Sharma T, Netz DJ, Pierik AJ, Wohlschlegel JA, Lill R. MMS19 assembles iron-sulfur proteins required for DNA metabolism and genomic integrity. Science. 2012 Jul 13;337(6091):195-9. PMID:22678362 doi:10.1126/science.1219723
↑ Prakash L, Prakash S. Three additional genes involved in pyrimidine dimer removal in Saccharomyces cerevisiae: RAD7, RAD14 and MMS19. Mol Gen Genet. 1979 Nov;176(3):351-9. PMID:392238 doi:10.1007/BF00333097
↑ Lauder S, Bankmann M, Guzder SN, Sung P, Prakash L, Prakash S. Dual requirement for the yeast MMS19 gene in DNA repair and RNA polymerase II transcription. Mol Cell Biol. 1996 Dec;16(12):6783-93. PMID:8943333 doi:10.1128/MCB.16.12.6783
↑ Lombaerts M, Tijsterman M, Verhage RA, Brouwer J. Saccharomyces cerevisiae mms19 mutants are deficient in transcription-coupled and global nucleotide excision repair. Nucleic Acids Res. 1997 Oct 15;25(20):3974-9. PMID:9321645 doi:10.1093/nar/25.20.3974

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OCA

[1] Kou H, Zhou Y, Gorospe RM, Wang Z. Mms19 protein functions in nucleotide excision repair by sustaining an adequate cellular concentration of the TFIIH component Rad3. Proc Natl Acad Sci U S A. 2008 Oct 14;105(41):15714-9. PMID:18836076 doi:10.1073/pnas.0710736105

[2] Stehling O, Vashisht AA, Mascarenhas J, Jonsson ZO, Sharma T, Netz DJ, Pierik AJ, Wohlschlegel JA, Lill R. MMS19 assembles iron-sulfur proteins required for DNA metabolism and genomic integrity. Science. 2012 Jul 13;337(6091):195-9. PMID:22678362 doi:10.1126/science.1219723

[3] Prakash L, Prakash S. Three additional genes involved in pyrimidine dimer removal in Saccharomyces cerevisiae: RAD7, RAD14 and MMS19. Mol Gen Genet. 1979 Nov;176(3):351-9. PMID:392238 doi:10.1007/BF00333097

[4] Lauder S, Bankmann M, Guzder SN, Sung P, Prakash L, Prakash S. Dual requirement for the yeast MMS19 gene in DNA repair and RNA polymerase II transcription. Mol Cell Biol. 1996 Dec;16(12):6783-93. PMID:8943333 doi:10.1128/MCB.16.12.6783

[5] Lombaerts M, Tijsterman M, Verhage RA, Brouwer J. Saccharomyces cerevisiae mms19 mutants are deficient in transcription-coupled and global nucleotide excision repair. Nucleic Acids Res. 1997 Oct 15;25(20):3974-9. PMID:9321645 doi:10.1093/nar/25.20.3974

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8usp is ON HOLD  until Paper Publication
+==Structural and biochemical investigations of a HEAT-repeat protein involved in the cytosolic iron-sulfur cluster assembly pathway==
+<StructureSection load='8usp' size='340' side='right'caption='[[8usp]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
-Authors: Vasquez, S., Drennan, C.L.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8usp]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces Saccharomyces]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8USP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8USP FirstGlance]. <br>
-Description: Structural and biochemical investigations of a HEAT-repeat protein involved in the cytosolic iron-sulfur cluster assembly pathway
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8usp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8usp OCA], [https://pdbe.org/8usp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8usp RCSB], [https://www.ebi.ac.uk/pdbsum/8usp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8usp ProSAT]</span></td></tr>
-[[Category: Drennan, C.L]]
+</table>
-[[Category: Vasquez, S]]
+== Function ==
+[https://www.uniprot.org/uniprot/MET18_YEAST MET18_YEAST] Key component of the cytosolic iron-sulfur protein assembly (CIA) machinery that mediates the incorporation of iron-sulfur cluster into apoproteins specifically involved in DNA metabolism and genomic integrity. Acts as an adapter between early-acting CIA components and a subset of cellular target iron-sulfur proteins such as RAD3/XPD and DNA2, thereby playing a key role in nucleotide excision repair (NER) and RNA polymerase II (POL II) transcription.<ref>PMID:18836076</ref> <ref>PMID:22678362</ref> <ref>PMID:392238</ref> <ref>PMID:8943333</ref> <ref>PMID:9321645</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Saccharomyces]]
+[[Category: Drennan CL]]
+[[Category: Vasquez S]]

8usp: Difference between revisions

Latest revision as of 23:16, 27 December 2023

Structural and biochemical investigations of a HEAT-repeat protein involved in the cytosolic iron-sulfur cluster assembly pathway

Structural highlights

Function

References

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