5zxd
From Proteopedia
(Difference between revisions)
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<StructureSection load='5zxd' size='340' side='right' caption='[[5zxd]], [[Resolution|resolution]] 2.29Å' scene=''> | <StructureSection load='5zxd' size='340' side='right' caption='[[5zxd]], [[Resolution|resolution]] 2.29Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5zxd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZXD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5zxd]] is a 2 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=5ZXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZXD FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABCF1, ABC50 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5zxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zxd OCA], [http://pdbe.org/5zxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zxd RCSB], [http://www.ebi.ac.uk/pdbsum/5zxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zxd ProSAT]</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=5zxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zxd OCA], [http://pdbe.org/5zxd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zxd RCSB], [http://www.ebi.ac.uk/pdbsum/5zxd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zxd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ABCF1_HUMAN ABCF1_HUMAN]] Isoform 2 is required for efficient Cap- and IRES-mediated mRNA translation initiation. Isoform 2 is not involved in the ribosome biogenesis.<ref>PMID:19570978</ref> | [[http://www.uniprot.org/uniprot/ABCF1_HUMAN ABCF1_HUMAN]] Isoform 2 is required for efficient Cap- and IRES-mediated mRNA translation initiation. Isoform 2 is not involved in the ribosome biogenesis.<ref>PMID:19570978</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Gene translation requires the correct selection of start codon AUG in mRNA. ATP-binding cassette subfamily F member 1 (ABCF1) plays a key role in the accuracy of start codon selection. However, the function of human ABCF1 is not clearly understood. Here, we solve the crystal structure of an ATP-bound wild-type human ABCF1 at 2.3-A resolution. The comparative studies indicate that the structure is in a pre-activation intermediate conformation. This conformation is stabilized by the interaction between ATP and protein. Thus, we propose that this conformation is an important step in the activation of ABCF1. This study extends our understanding of ABC (ATP-binding cassette) protein activation at the molecular level. | ||
| + | |||
| + | Crystal Structure of ATP-Bound Human ABCF1 Demonstrates a Unique Conformation of ABC Proteins.,Qu L, Jiang Y, Cheng C, Wu D, Meng B, Chen Z, Zhu Y, Shaw N, Ouyang S, Liu ZJ Structure. 2018 Jun 12. pii: S0969-2126(18)30206-5. doi:, 10.1016/j.str.2018.05.019. PMID:30017566<ref>PMID:30017566</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5zxd" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Jiang, Y]] | [[Category: Jiang, Y]] | ||
[[Category: Liu, Z J]] | [[Category: Liu, Z J]] | ||
Current revision
Crystal structure of ATP-bound human ABCF1
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Categories: Human | Jiang, Y | Liu, Z J | Qu, L | Regulator | Translation
