1x9z
From Proteopedia
(New page: 200px<br /><applet load="1x9z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x9z, resolution 2.10Å" /> '''Crystal structure of...) |
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| - | [[Image:1x9z.jpg|left|200px]]<br /><applet load="1x9z" size=" | + | [[Image:1x9z.jpg|left|200px]]<br /><applet load="1x9z" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1x9z, resolution 2.10Å" /> | caption="1x9z, resolution 2.10Å" /> | ||
'''Crystal structure of the MutL C-terminal domain'''<br /> | '''Crystal structure of the MutL C-terminal domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | MutL assists the mismatch recognition protein MutS to initiate and | + | 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 Structure== | ==About this Structure== | ||
| - | 1X9Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CL, NA, GOL and IPA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1X9Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=GOL:'>GOL</scene> and <scene name='pdbligand=IPA:'>IPA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9Z OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Guarne, A.]] | [[Category: Guarne, A.]] | ||
[[Category: Hu, X.]] | [[Category: Hu, X.]] | ||
| - | [[Category: Miller, J | + | [[Category: Miller, J H.]] |
[[Category: Ramon-Maiques, S.]] | [[Category: Ramon-Maiques, S.]] | ||
| - | [[Category: Wolff, E | + | [[Category: Wolff, E M.]] |
[[Category: Yang, W.]] | [[Category: Yang, W.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: dimer]] | [[Category: dimer]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:52:40 2008'' |
Revision as of 13:52, 21 February 2008
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Crystal structure of the MutL C-terminal domain
Overview
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 Structure
1X9Z is a Single protein structure of sequence from Escherichia coli with , , and as ligands. Full crystallographic information is available from OCA.
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:15470502
Page seeded by OCA on Thu Feb 21 15:52:40 2008
Categories: Escherichia coli | Single protein | Ghirlando, R. | Guarne, A. | Hu, X. | Miller, J H. | Ramon-Maiques, S. | Wolff, E M. | Yang, W. | CL | GOL | IPA | NA | Alpha-beta fold | Dimer
