1bkn: Difference between revisions

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[[Image:1bkn.~~gif~~|left|200px]]

[[Image:1bkn.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF AN N-TERMINAL 40KD FRAGMENT OF E. COLI DNA MISMATCH REPAIR PROTEIN MUTL~~'''~~

===CRYSTAL STRUCTURE OF AN N-TERMINAL 40KD FRAGMENT OF E. COLI DNA MISMATCH REPAIR PROTEIN MUTL===

~~==Overview==~~

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MutL and its homologs are essential for DNA mismatch repair. Mutations in genes encoding human homologs of MutL cause multiorgan cancer susceptibility. We have determined the crystal structure of a 40 kDa N-terminal fragment of E. coli MutL that retains all of the conserved residues in the MutL family. The ~~structure of MutL is homologous to that of an ATPase-containing fragment of DNA gyrase. We have demonstrated that MutL binds and hydrolyzes ATP to ADP and Pi. Mutations in~~ the ~~MutL family that cause deficiencies in DNA mismatch repair and a predisposition~~ to ~~cancer mainly occur in~~ the ~~putative ATP-binding site~~. ~~We provide evidence that the flexible~~, ~~yet conserved, loops surrounding this ATP-binding site undergo conformational changes upon ATP hydrolysis thereby modulating interactions between MutL and other components of~~ the ~~repair machinery~~.

The line below this paragraph, {{ABSTRACT_PUBMED_9827806}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9827806 is the PubMed ID number.

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==About this Structure==

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[[Category: Dna binding]]

[[Category: Dna repair]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 11~~:38:12 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:18:52 2008''

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-[[Image:1bkn.gif|left|200px]]
+{{Seed}}
+[[Image:1bkn.png|left|200px]]
 <!--
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 {{STRUCTURE_1bkn|  PDB=1bkn  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF AN N-TERMINAL 40KD FRAGMENT OF E. COLI DNA MISMATCH REPAIR PROTEIN MUTL'''
+===CRYSTAL STRUCTURE OF AN N-TERMINAL 40KD FRAGMENT OF E. COLI DNA MISMATCH REPAIR PROTEIN MUTL===
-==Overview==
+<!--
-MutL and its homologs are essential for DNA mismatch repair. Mutations in genes encoding human homologs of MutL cause multiorgan cancer susceptibility. We have determined the crystal structure of a 40 kDa N-terminal fragment of E. coli MutL that retains all of the conserved residues in the MutL family. The structure of MutL is homologous to that of an ATPase-containing fragment of DNA gyrase. We have demonstrated that MutL binds and hydrolyzes ATP to ADP and Pi. Mutations in the MutL family that cause deficiencies in DNA mismatch repair and a predisposition to cancer mainly occur in the putative ATP-binding site. We provide evidence that the flexible, yet conserved, loops surrounding this ATP-binding site undergo conformational changes upon ATP hydrolysis thereby modulating interactions between MutL and other components of the repair machinery.
+The line below this paragraph, {{ABSTRACT_PUBMED_9827806}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9827806 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9827806}}
 ==About this Structure==
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 [[Category: Dna binding]]
 [[Category: Dna repair]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:38:12 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:18:52 2008''