1x9z: Difference between revisions
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'''Crystal structure of the MutL C-terminal domain''' | {{Structure | ||
|PDB= 1x9z |SIZE=350|CAPTION= <scene name='initialview01'>1x9z</scene>, resolution 2.10Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> and <scene name='pdbligand=IPA:ISOPROPYL ALCOHOL'>IPA</scene> | |||
|ACTIVITY= | |||
|GENE= mutL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Crystal structure of the MutL C-terminal domain''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1X9Z is a [ | 1X9Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9Z OCA]. | ||
==Reference== | ==Reference== | ||
Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repair., Guarne A, Ramon-Maiques S, Wolff EM, Ghirlando R, Hu X, Miller JH, Yang W, EMBO J. 2004 Oct 27;23(21):4134-45. Epub 2004 Oct 7. PMID:[http:// | Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repair., Guarne A, Ramon-Maiques S, Wolff EM, Ghirlando R, Hu X, Miller JH, Yang W, EMBO J. 2004 Oct 27;23(21):4134-45. Epub 2004 Oct 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15470502 15470502] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: dimer]] | [[Category: dimer]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:07:02 2008'' | ||
Revision as of 16:07, 20 March 2008
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| , resolution 2.10Å | |||||||
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| Ligands: | , , and | ||||||
| Gene: | mutL (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the MutL C-terminal domain
OverviewOverview
MutL assists the mismatch recognition protein MutS to initiate and coordinate mismatch repair in species ranging from bacteria to humans. The MutL N-terminal ATPase domain is highly conserved, but the C-terminal region shares little sequence similarity among MutL homologs. We report here the crystal structure of the Escherichia coli MutL C-terminal dimerization domain and the likelihood of its conservation among MutL homologs. A 100-residue proline-rich linker between the ATPase and dimerization domains, which generates a large central cavity in MutL dimers, tolerates sequence substitutions and deletions of one-third of its length with no functional consequences in vivo or in vitro. Along the surface of the central cavity, residues essential for DNA binding are located in both the N- and C-terminal domains. Each domain of MutL interacts with UvrD helicase and is required for activating the helicase activity. The DNA-binding capacity of MutL is correlated with the level of UvrD activation. A model of how MutL utilizes its ATPase and DNA-binding activities to mediate mismatch-dependent activation of MutH endonuclease and UvrD helicase is proposed.
About this StructureAbout this Structure
1X9Z is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repair., Guarne A, Ramon-Maiques S, Wolff EM, Ghirlando R, Hu X, Miller JH, Yang W, EMBO J. 2004 Oct 27;23(21):4134-45. Epub 2004 Oct 7. PMID:15470502
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