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| | <StructureSection load='4nho' size='340' side='right'caption='[[4nho]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='4nho' size='340' side='right'caption='[[4nho]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4nho]] is a 1 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=4NHO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NHO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4nho]] is a 1 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=4NHO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NHO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</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=4nho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nho OCA], [https://pdbe.org/4nho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nho RCSB], [https://www.ebi.ac.uk/pdbsum/4nho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nho ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDX23 ([http://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/RNA_helicase RNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </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=4nho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nho OCA], [http://pdbe.org/4nho PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nho RCSB], [http://www.ebi.ac.uk/pdbsum/4nho PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nho ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DDX23_HUMAN DDX23_HUMAN]] Involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation.<ref>PMID:18425142</ref> | + | [https://www.uniprot.org/uniprot/DDX23_HUMAN DDX23_HUMAN] Involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation.<ref>PMID:18425142</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: RNA helicase]]
| + | [[Category: Ficner R]] |
| - | [[Category: Ficner, R]] | + | [[Category: Moehlmann S]] |
| - | [[Category: Moehlmann, S]] | + | [[Category: Neumann P]] |
| - | [[Category: Neumann, P]] | + | |
| - | [[Category: Dead-box]]
| + | |
| - | [[Category: Helicase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
DDX23_HUMAN Involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation.[1]
Publication Abstract from PubMed
The DEAD-box protein Prp28 is essential for pre-mRNA splicing as it plays a key role in the formation of an active spliceosome. Prp28 participates in the release of the U1 snRNP from the 5'-splice site during association of the U5.U4/U6 tri-snRNP, which is a crucial step in the transition from a pre-catalytic spliceosome to an activated spliceosome. Here, it is demonstrated that the purified helicase domain of human Prp28 (hPrp28DeltaN) binds ADP, whereas binding of ATP and ATPase activity could not be detected. ATP binding could not be observed for purified full-length hPrp28 either, but within an assembled spliceosomal complex hPrp28 gains ATP-binding activity. In order to understand the structural basis for the ATP-binding deficiency of isolated hPrp28, the crystal structure of hPrp28DeltaN was determined at 2.0 A resolution. In the crystal the helicase domain adopts a wide-open conformation, as the two RecA-like domains are extraordinarily displaced from the productive ATPase conformation. Binding of ATP is hindered by a closed conformation of the P-loop, which occupies the space required for the gamma-phosphate of ATP.
Structural and functional analysis of the human spliceosomal DEAD-box helicase Prp28.,Mohlmann S, Mathew R, Neumann P, Schmitt A, Luhrmann R, Ficner R Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1622-30. doi:, 10.1107/S1399004714006439. Epub 2014 May 24. PMID:24914973[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mathew R, Hartmuth K, Mohlmann S, Urlaub H, Ficner R, Luhrmann R. Phosphorylation of human PRP28 by SRPK2 is required for integration of the U4/U6-U5 tri-snRNP into the spliceosome. Nat Struct Mol Biol. 2008 May;15(5):435-43. doi: 10.1038/nsmb.1415. Epub 2008 Apr, 20. PMID:18425142 doi:http://dx.doi.org/10.1038/nsmb.1415
- ↑ Mohlmann S, Mathew R, Neumann P, Schmitt A, Luhrmann R, Ficner R. Structural and functional analysis of the human spliceosomal DEAD-box helicase Prp28. Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1622-30. doi:, 10.1107/S1399004714006439. Epub 2014 May 24. PMID:24914973 doi:http://dx.doi.org/10.1107/S1399004714006439
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