2j8q: Difference between revisions

Latest revision as of 14:38, 13 December 2023

Crystal structure of human cleavage and polyadenylation specificity factor 5 (CPSF5) in complex with a sulphate ion.

Structural highlights

2j8q is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:	SO4
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CPSF5_HUMAN Component of the cleavage factor Im (CFIm) complex that plays a key role in pre-mRNA 3'-processing. Involved in association with CPSF6 or CPSF7 in pre-MRNA 3'-end poly(A) site cleavage and poly(A) addition. NUDT21/CPSF5 binds to cleavage and polyadenylation RNA substrates. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA. Binds to, but does not hydrolyze mono- and di-adenosine nucleotides. May have a role in mRNA export.^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Ruegsegger U, Blank D, Keller W. Human pre-mRNA cleavage factor Im is related to spliceosomal SR proteins and can be reconstituted in vitro from recombinant subunits. Mol Cell. 1998 Jan;1(2):243-53. PMID:9659921
↑ Ruegsegger U, Beyer K, Keller W. Purification and characterization of human cleavage factor Im involved in the 3' end processing of messenger RNA precursors. J Biol Chem. 1996 Mar 15;271(11):6107-13. PMID:8626397
↑ Brown KM, Gilmartin GM. A mechanism for the regulation of pre-mRNA 3' processing by human cleavage factor Im. Mol Cell. 2003 Dec;12(6):1467-76. PMID:14690600
↑ Kim S, Yamamoto J, Chen Y, Aida M, Wada T, Handa H, Yamaguchi Y. Evidence that cleavage factor Im is a heterotetrameric protein complex controlling alternative polyadenylation. Genes Cells. 2010 Sep 1;15(9):1003-13. doi: 10.1111/j.1365-2443.2010.01436.x., Epub 2010 Jul 29. PMID:20695905 doi:10.1111/j.1365-2443.2010.01436.x
↑ Yang Q, Gilmartin GM, Doublie S. Structural basis of UGUA recognition by the Nudix protein CFI(m)25 and implications for a regulatory role in mRNA 3' processing. Proc Natl Acad Sci U S A. 2010 Jun 1;107(22):10062-7. Epub 2010 May 17. PMID:20479262
↑ Yang Q, Coseno M, Gilmartin GM, Doublie S. Crystal Structure of a Human Cleavage Factor CFI(m)25/CFI(m)68/RNA Complex Provides an Insight into Poly(A) Site Recognition and RNA Looping. Structure. 2011 Feb 2. PMID:21295486 doi:10.1016/j.str.2010.12.021

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Ruegsegger U, Blank D, Keller W. Human pre-mRNA cleavage factor Im is related to spliceosomal SR proteins and can be reconstituted in vitro from recombinant subunits. Mol Cell. 1998 Jan;1(2):243-53. PMID:9659921

[2] Ruegsegger U, Beyer K, Keller W. Purification and characterization of human cleavage factor Im involved in the 3' end processing of messenger RNA precursors. J Biol Chem. 1996 Mar 15;271(11):6107-13. PMID:8626397

[3] Brown KM, Gilmartin GM. A mechanism for the regulation of pre-mRNA 3' processing by human cleavage factor Im. Mol Cell. 2003 Dec;12(6):1467-76. PMID:14690600

[4] Kim S, Yamamoto J, Chen Y, Aida M, Wada T, Handa H, Yamaguchi Y. Evidence that cleavage factor Im is a heterotetrameric protein complex controlling alternative polyadenylation. Genes Cells. 2010 Sep 1;15(9):1003-13. doi: 10.1111/j.1365-2443.2010.01436.x., Epub 2010 Jul 29. PMID:20695905 doi:10.1111/j.1365-2443.2010.01436.x

[5] Yang Q, Gilmartin GM, Doublie S. Structural basis of UGUA recognition by the Nudix protein CFI(m)25 and implications for a regulatory role in mRNA 3' processing. Proc Natl Acad Sci U S A. 2010 Jun 1;107(22):10062-7. Epub 2010 May 17. PMID:20479262

[6] Yang Q, Coseno M, Gilmartin GM, Doublie S. Crystal Structure of a Human Cleavage Factor CFI(m)25/CFI(m)68/RNA Complex Provides an Insight into Poly(A) Site Recognition and RNA Looping. Structure. 2011 Feb 2. PMID:21295486 doi:10.1016/j.str.2010.12.021

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[2]

[3]

[4]

[5]

[6]

@@ Line 1: / Line 1: @@
-[[Image:2j8q.gif|left|200px]]<br />
-<applet load="2j8q" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2j8q, resolution 2.30&Aring;" />
-'''CRYSTAL STRUCTURE OF HUMAN CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR 5 (CPSF5) IN COMPLEX WITH A SULPHATE ION.'''<br />
-==About this Structure==
+==Crystal structure of human cleavage and polyadenylation specificity factor 5 (CPSF5) in complex with a sulphate ion.==
-J8Q is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J8Q OCA]].
+<StructureSection load='2j8q' size='340' side='right'caption='[[2j8q]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2j8q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J8Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J8Q FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2j8q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j8q OCA], [https://pdbe.org/2j8q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j8q RCSB], [https://www.ebi.ac.uk/pdbsum/2j8q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j8q ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CPSF5_HUMAN CPSF5_HUMAN] Component of the cleavage factor Im (CFIm) complex that plays a key role in pre-mRNA 3'-processing. Involved in association with CPSF6 or CPSF7 in pre-MRNA 3'-end poly(A) site cleavage and poly(A) addition. NUDT21/CPSF5 binds to cleavage and polyadenylation RNA substrates. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA. Binds to, but does not hydrolyze mono- and di-adenosine nucleotides. May have a role in mRNA export.<ref>PMID:9659921</ref> <ref>PMID:8626397</ref> <ref>PMID:14690600</ref> <ref>PMID:20695905</ref> <ref>PMID:20479262</ref> <ref>PMID:21295486</ref>
+== 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/j8/2j8q_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=2j8q ConSurf].
+<div style="clear:both"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Arrowsmith, C.]]
+[[Category: Arrowsmith C]]
-[[Category: Berg, S.Van.Den.]]
+[[Category: Berglund H]]
-[[Category: Berglund, H.]]
+[[Category: Busam R]]
-[[Category: Busam, R.]]
+[[Category: Collins R]]
-[[Category: Collins, R.]]
+[[Category: Edwards A]]
-[[Category: Edwards, A.]]
+[[Category: Ericsson UB]]
-[[Category: Ericsson, U.B.]]
+[[Category: Flodin S]]
-[[Category: Flodin, S.]]
+[[Category: Flores A]]
-[[Category: Flores, A.]]
+[[Category: Graslund S]]
-[[Category: Graslund, S.]]
+[[Category: Hallberg BM]]
-[[Category: Hallberg, B.M.]]
+[[Category: Hammarstrom M]]
-[[Category: Hammarstrom, M.]]
+[[Category: Hogbom M]]
-[[Category: Hogbom, M.]]
+[[Category: Holmberg SL]]
-[[Category: Holmberg, S.L.]]
+[[Category: Johansson I]]
-[[Category: Johansson, I.]]
+[[Category: Karlberg T]]
-[[Category: Karlberg, T.]]
+[[Category: Kosinska U]]
-[[Category: Kosinska, U.]]
+[[Category: Kotenyova T]]
-[[Category: Kotenyova, T.]]
+[[Category: Magnusdottir A]]
-[[Category: Magnusdottir, A.]]
+[[Category: Moche M]]
-[[Category: Moche, M.]]
+[[Category: Nilsson ME]]
-[[Category: Nilsson, M.E.]]
+[[Category: Nilsson-Ehle P]]
-[[Category: Nilsson-Ehle, P.]]
+[[Category: Nordlund P]]
-[[Category: Nordlund, P.]]
+[[Category: Nyman T]]
-[[Category: Nyman, T.]]
+[[Category: Ogg D]]
-[[Category: Ogg, D.]]
+[[Category: Persson C]]
-[[Category: Persson, C.]]
+[[Category: Sagemark J]]
-[[Category: Sagemark, J.]]
+[[Category: Stenmark P]]
-[[Category: Stenmark, P.]]
+[[Category: Sundstrom M]]
-[[Category: Sundstrom, M.]]
+[[Category: Thorsell AG]]
-[[Category: Thorsell, A.G.]]
+[[Category: Uppenberg J]]
-[[Category: Uppenberg, J.]]
+[[Category: Upsten M]]
-[[Category: Upsten, M.]]
+[[Category: Van Den Berg S]]
-[[Category: Wallden, K.]]
+[[Category: Wallden K]]
-[[Category: Weigelt, J.]]
+[[Category: Weigelt J]]
-[[Category: Welin, M.]]
+[[Category: Welin M]]
-[[Category: SO4]]
-[[Category: 3'mrna cleavage and polyadenylation factor]]
-[[Category: mrna processing]]
-[[Category: nuclear protein]]
-[[Category: phosphorylation]]
-[[Category: rna-binding]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 22:03:54 2007''

2j8q: Difference between revisions

Latest revision as of 14:38, 13 December 2023

Crystal structure of human cleavage and polyadenylation specificity factor 5 (CPSF5) in complex with a sulphate ion.

Structural highlights

Function

Evolutionary Conservation

References

Contents

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