1b63

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[[Image:1b63.gif|left|200px]]
[[Image:1b63.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1b63 |SIZE=350|CAPTION= <scene name='initialview01'>1b63</scene>, resolution 1.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1b63", 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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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= MUTL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_1b63| PDB=1b63 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b63 OCA], [http://www.ebi.ac.uk/pdbsum/1b63 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b63 RCSB]</span>
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}}
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'''MUTL COMPLEXED WITH ADPNP'''
'''MUTL COMPLEXED WITH ADPNP'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Yang, W.]]
[[Category: Yang, W.]]
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[[Category: atpase]]
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[[Category: Atpase]]
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[[Category: dna mismatch repair]]
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[[Category: Dna mismatch repair]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:07:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:54:22 2008''
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Revision as of 08:07, 2 May 2008

Image:1b63.gif

Template:STRUCTURE 1b63

MUTL COMPLEXED WITH ADPNP


Overview

The MutL DNA mismatch repair protein has recently been shown to be an ATPase and to belong to an emerging ATPase superfamily that includes DNA topoisomerase II and Hsp90. We report here the crystal structures of a 40 kDa ATPase fragment of E. coli MutL (LN40) complexed with a substrate analog, ADPnP, and with product ADP. More than 60 residues that are disordered in the apoprotein structure become ordered and contribute to both ADPnP binding and dimerization of LN40. Hydrolysis of ATP, signified by subsequent release of the gamma-phosphate, releases two key loops and leads to dissociation of the LN40 dimer. Dimerization of the LN40 region is required for and is the rate-limiting step in ATP hydrolysis by MutL. The ATPase activity of MutL is stimulated by DNA and likely acts as a switch to coordinate DNA mismatch repair.

About this Structure

1B63 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair., Ban C, Junop M, Yang W, Cell. 1999 Apr 2;97(1):85-97. PMID:10199405 Page seeded by OCA on Fri May 2 11:07:05 2008

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