This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1x9z

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1x9z.jpg|left|200px]]<br /><applet load="1x9z" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1x9z.jpg|left|200px]]
-
caption="1x9z, resolution 2.10&Aring;" />
+
 
-
'''Crystal structure of the MutL C-terminal domain'''<br />
+
{{Structure
 +
|PDB= 1x9z |SIZE=350|CAPTION= <scene name='initialview01'>1x9z</scene>, resolution 2.10&Aring;
 +
|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==
Line 7: Line 16:
==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 <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].
+
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15470502 15470502]
+
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]]
Line 27: Line 36:
[[Category: dimer]]
[[Category: dimer]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:52:40 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:07:02 2008''

Revision as of 13:07, 20 March 2008


PDB ID 1x9z

Drag the structure with the mouse to rotate
, resolution 2.10Å
Ligands: , , and
Gene: mutL (Escherichia coli)
Coordinates: save as pdb, mmCIF, xml



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. 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 Mar 20 15:07:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools