3puf

From Proteopedia

(Difference between revisions)

Revision as of 08:55, 25 May 2022

Crystal structure of human RNase H2 complex

Structural highlights

3puf is a 18 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	RNASEH2A, RNASEHI, RNHIA (HUMAN), RNASEH2B, DLEU8 (HUMAN), RNASEH2C, AYP1 (HUMAN)
Activity:	Ribonuclease H, with EC number 3.1.26.4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[RNH2A_HUMAN] Aicardi-Goutieres syndrome. The disease is caused by mutations affecting the gene represented in this entry. [RNH2C_HUMAN] Aicardi-Goutieres syndrome. The disease is caused by mutations affecting the gene represented in this entry. [RNH2B_HUMAN] Aicardi-Goutieres syndrome. The disease is caused by mutations affecting the gene represented in this entry.

Function

[RNH2A_HUMAN] Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.^[1] ^[2] [RNH2C_HUMAN] Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.^[3] ^[4] [RNH2B_HUMAN] Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.^[5] ^[6]

Publication Abstract from PubMed

RNase H2 cleaves RNA sequences that are part of RNA/DNA hybrids or that are incorporated into DNA, thus, preventing genomic instability and the accumulation of aberrant nucleic acid, which in humans induces Aicardi-Goutieres syndrome, a severe autoimmune disorder. The 3.1 A crystal structure of human RNase H2 presented here allowed us to map the positions of all 29 mutations found in Aicardi-Goutieres syndrome patients, several of which were not visible in the previously reported mouse RNase H2. We propose the possible effects of these mutations on the protein stability and function. Bacterial and eukaryotic RNases H2 differ in composition and substrate specificity. Bacterial RNases H2 are monomeric proteins and homologs of the eukaryotic RNases H2 catalytic subunit, which in addition possesses two accessory proteins. The eukaryotic RNase H2 heterotrimeric complex recognizes RNA/DNA hybrids and (5')RNA-DNA(3')/DNA junction hybrids as substrates with similar efficiency, whereas bacterial RNases H2 are highly specialized in the recognition of the (5')RNA-DNA(3') junction and very poorly cleave RNA/DNA hybrids in the presence of Mg(2+) ions. Using the crystal structure of the Thermotoga maritima RNase H2-substrate complex, we modeled the human RNase H2-substrate complex and verified the model by mutational analysis. Our model indicates that the difference in substrate preference stems from the different position of the crucial tyrosine residue involved in substrate binding and recognition.

The structural and biochemical characterization of human RNase H2 complex reveals the molecular basis for substrate recognition and Aicardi-Goutieres syndrome defects.,Figiel M, Chon H, Cerritelli SM, Cybulska M, Crouch RJ, Nowotny M J Biol Chem. 2011 Mar 25;286(12):10540-50. Epub 2010 Dec 22. PMID:21177858^[7]

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

References

↑ Crow YJ, Leitch A, Hayward BE, Garner A, Parmar R, Griffith E, Ali M, Semple C, Aicardi J, Babul-Hirji R, Baumann C, Baxter P, Bertini E, Chandler KE, Chitayat D, Cau D, Dery C, Fazzi E, Goizet C, King MD, Klepper J, Lacombe D, Lanzi G, Lyall H, Martinez-Frias ML, Mathieu M, McKeown C, Monier A, Oade Y, Quarrell OW, Rittey CD, Rogers RC, Sanchis A, Stephenson JB, Tacke U, Till M, Tolmie JL, Tomlin P, Voit T, Weschke B, Woods CG, Lebon P, Bonthron DT, Ponting CP, Jackson AP. Mutations in genes encoding ribonuclease H2 subunits cause Aicardi-Goutieres syndrome and mimic congenital viral brain infection. Nat Genet. 2006 Aug;38(8):910-6. Epub 2006 Jul 16. PMID:16845400 doi:http://dx.doi.org/10.1038/ng1842
↑ Figiel M, Chon H, Cerritelli SM, Cybulska M, Crouch RJ, Nowotny M. The structural and biochemical characterization of human RNase H2 complex reveals the molecular basis for substrate recognition and Aicardi-Goutieres syndrome defects. J Biol Chem. 2011 Mar 25;286(12):10540-50. Epub 2010 Dec 22. PMID:21177858 doi:10.1074/jbc.M110.181974
↑ Crow YJ, Leitch A, Hayward BE, Garner A, Parmar R, Griffith E, Ali M, Semple C, Aicardi J, Babul-Hirji R, Baumann C, Baxter P, Bertini E, Chandler KE, Chitayat D, Cau D, Dery C, Fazzi E, Goizet C, King MD, Klepper J, Lacombe D, Lanzi G, Lyall H, Martinez-Frias ML, Mathieu M, McKeown C, Monier A, Oade Y, Quarrell OW, Rittey CD, Rogers RC, Sanchis A, Stephenson JB, Tacke U, Till M, Tolmie JL, Tomlin P, Voit T, Weschke B, Woods CG, Lebon P, Bonthron DT, Ponting CP, Jackson AP. Mutations in genes encoding ribonuclease H2 subunits cause Aicardi-Goutieres syndrome and mimic congenital viral brain infection. Nat Genet. 2006 Aug;38(8):910-6. Epub 2006 Jul 16. PMID:16845400 doi:http://dx.doi.org/10.1038/ng1842
↑ Figiel M, Chon H, Cerritelli SM, Cybulska M, Crouch RJ, Nowotny M. The structural and biochemical characterization of human RNase H2 complex reveals the molecular basis for substrate recognition and Aicardi-Goutieres syndrome defects. J Biol Chem. 2011 Mar 25;286(12):10540-50. Epub 2010 Dec 22. PMID:21177858 doi:10.1074/jbc.M110.181974
↑ Figiel M, Chon H, Cerritelli SM, Cybulska M, Crouch RJ, Nowotny M. The structural and biochemical characterization of human RNase H2 complex reveals the molecular basis for substrate recognition and Aicardi-Goutieres syndrome defects. J Biol Chem. 2011 Mar 25;286(12):10540-50. Epub 2010 Dec 22. PMID:21177858 doi:10.1074/jbc.M110.181974
↑ Crow YJ, Leitch A, Hayward BE, Garner A, Parmar R, Griffith E, Ali M, Semple C, Aicardi J, Babul-Hirji R, Baumann C, Baxter P, Bertini E, Chandler KE, Chitayat D, Cau D, Dery C, Fazzi E, Goizet C, King MD, Klepper J, Lacombe D, Lanzi G, Lyall H, Martinez-Frias ML, Mathieu M, McKeown C, Monier A, Oade Y, Quarrell OW, Rittey CD, Rogers RC, Sanchis A, Stephenson JB, Tacke U, Till M, Tolmie JL, Tomlin P, Voit T, Weschke B, Woods CG, Lebon P, Bonthron DT, Ponting CP, Jackson AP. Mutations in genes encoding ribonuclease H2 subunits cause Aicardi-Goutieres syndrome and mimic congenital viral brain infection. Nat Genet. 2006 Aug;38(8):910-6. Epub 2006 Jul 16. PMID:16845400 doi:http://dx.doi.org/10.1038/ng1842
↑ Figiel M, Chon H, Cerritelli SM, Cybulska M, Crouch RJ, Nowotny M. The structural and biochemical characterization of human RNase H2 complex reveals the molecular basis for substrate recognition and Aicardi-Goutieres syndrome defects. J Biol Chem. 2011 Mar 25;286(12):10540-50. Epub 2010 Dec 22. PMID:21177858 doi:10.1074/jbc.M110.181974

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal structure of human RNase H2 complex==
-<StructureSection load='3puf' size='340' side='right' caption='[[3puf]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+<StructureSection load='3puf' size='340' side='right'caption='[[3puf]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3puf]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PUF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PUF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3puf]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PUF FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RNASEH2A, RNASEHI, RNHIA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RNASEH2B, DLEU8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RNASEH2C, AYP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RNASEH2A, RNASEHI, RNHIA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RNASEH2B, DLEU8 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), RNASEH2C, AYP1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] </span></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=3puf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3puf OCA], [http://pdbe.org/3puf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3puf RCSB], [http://www.ebi.ac.uk/pdbsum/3puf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3puf ProSAT]</span></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=3puf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3puf OCA], [https://pdbe.org/3puf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3puf RCSB], [https://www.ebi.ac.uk/pdbsum/3puf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3puf ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/RNH2A_HUMAN RNH2A_HUMAN]] Aicardi-Goutieres syndrome. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/RNH2C_HUMAN RNH2C_HUMAN]] Aicardi-Goutieres syndrome. The disease is caused by mutations affecting the gene represented in this entry. [[http://www.uniprot.org/uniprot/RNH2B_HUMAN RNH2B_HUMAN]] Aicardi-Goutieres syndrome. The disease is caused by mutations affecting the gene represented in this entry.
+[[https://www.uniprot.org/uniprot/RNH2A_HUMAN RNH2A_HUMAN]] Aicardi-Goutieres syndrome. The disease is caused by mutations affecting the gene represented in this entry. [[https://www.uniprot.org/uniprot/RNH2C_HUMAN RNH2C_HUMAN]] Aicardi-Goutieres syndrome. The disease is caused by mutations affecting the gene represented in this entry. [[https://www.uniprot.org/uniprot/RNH2B_HUMAN RNH2B_HUMAN]] Aicardi-Goutieres syndrome. The disease is caused by mutations affecting the gene represented in this entry.
 == Function ==
-[[http://www.uniprot.org/uniprot/RNH2A_HUMAN RNH2A_HUMAN]] Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.<ref>PMID:16845400</ref> <ref>PMID:21177858</ref>  [[http://www.uniprot.org/uniprot/RNH2C_HUMAN RNH2C_HUMAN]] Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.<ref>PMID:16845400</ref> <ref>PMID:21177858</ref>  [[http://www.uniprot.org/uniprot/RNH2B_HUMAN RNH2B_HUMAN]] Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.<ref>PMID:21177858</ref> <ref>PMID:16845400</ref>
+[[https://www.uniprot.org/uniprot/RNH2A_HUMAN RNH2A_HUMAN]] Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.<ref>PMID:16845400</ref> <ref>PMID:21177858</ref>  [[https://www.uniprot.org/uniprot/RNH2C_HUMAN RNH2C_HUMAN]] Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.<ref>PMID:16845400</ref> <ref>PMID:21177858</ref>  [[https://www.uniprot.org/uniprot/RNH2B_HUMAN RNH2B_HUMAN]] Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.<ref>PMID:21177858</ref> <ref>PMID:16845400</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 ==See Also==
-*[[Ribonuclease|Ribonuclease]]
+*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
-*[[Temp|Temp]]
 == References ==
 <references/>
@@ Line 30: / Line 29: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Ribonuclease H]]
 [[Category: Cerritelli, S M]]

3puf

From Proteopedia

Revision as of 08:55, 25 May 2022

Crystal structure of human RNase H2 complex

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

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