1xml

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[[Image:1xml.gif|left|200px]]
[[Image:1xml.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1xml |SIZE=350|CAPTION= <scene name='initialview01'>1xml</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1xml", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1xml| PDB=1xml | SCENE= }}
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|RELATEDENTRY=[[1xmm|1XMM]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xml OCA], [http://www.ebi.ac.uk/pdbsum/1xml PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xml RCSB]</span>
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}}
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'''Structure of human Dcps'''
'''Structure of human Dcps'''
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[[Category: Chen, N.]]
[[Category: Chen, N.]]
[[Category: Song, H.]]
[[Category: Song, H.]]
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[[Category: scavenger decapping enzyme]]
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[[Category: Scavenger decapping enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:13:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:51:45 2008''
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Revision as of 12:13, 3 May 2008

Template:STRUCTURE 1xml

Structure of human Dcps


Overview

Eukaryotic cells utilize DcpS, a scavenger decapping enzyme, to degrade the residual cap structure following 3'-5' mRNA decay, thereby preventing the premature decapping of the capped long mRNA and misincorporation of methylated nucleotides in nucleic acids. We report the structures of DcpS in ligand-free form and in a complex with m7GDP. apo-DcpS is a symmetric dimer, strikingly different from the asymmetric dimer observed in the structures of DcpS with bound cap analogues. In contrast, and similar to the m7GpppG-DcpS complex, DcpS with bound m7GDP is an asymmetric dimer in which the closed state appears to be the substrate-bound complex, whereas the open state mimics the product-bound complex. Comparisons of these structures revealed conformational changes of both the N-terminal swapped-dimeric domain and the cap-binding pocket upon cap binding. Moreover, Tyr273 in the cap-binding pocket displays remarkable conformational changes upon cap binding. Mutagenesis and biochemical analysis suggest that Tyr273 seems to play an important role in cap binding and product release. Examination of the crystallographic B-factors indicates that the N-terminal domain in apo-DcpS is inherently flexible, and in a dynamic state ready for substrate binding and product release.

About this Structure

1XML is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structures of human DcpS in ligand-free and m7GDP-bound forms suggest a dynamic mechanism for scavenger mRNA decapping., Chen N, Walsh MA, Liu Y, Parker R, Song H, J Mol Biol. 2005 Apr 8;347(4):707-18. PMID:15769464 Page seeded by OCA on Sat May 3 15:13:42 2008

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