DNA mismatch repair protein

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:56, 13 June 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
-
<StructureSection load='7ai5' size='340' side='right' caption='E. coli MutS complex with DNA and ATP (PDB id [[7ai5]])' scene=''>
+
<StructureSection load='7ai5' size='340' side='right' caption='E. coli MutS complex with DNA and ATP (PDB id [[7ai5]])' scene='91/916389/Cv/1'>
Line 5: Line 5:
'''DNA mismatch repair proteins''' are key players in genomic stability by signalling mismatches occurring during DNA replication and recombination<ref>PMID:18157157</ref> .<br/>
'''DNA mismatch repair proteins''' are key players in genomic stability by signalling mismatches occurring during DNA replication and recombination<ref>PMID:18157157</ref> .<br/>
-
'''MutS''' is prokaryotic and recognizes base-base mismatches and small insertion/deletion mispairs<ref>PMID:11048711</ref> .<br />
+
*'''MutS''' is prokaryotic and recognizes base-base mismatches and small insertion/deletion mispairs<ref>PMID:11048711</ref> .<br />
-
'''MutL''' enhances recognition of mismatches<ref>PMID:15470502</ref> <br />
+
*'''MutL''' enhances recognition of mismatches<ref>PMID:15470502</ref> <br />
-
'''MutH''' is the eukaryotic homolog of MutS <br />
+
*'''MutH''' is the eukaryotic homolog of MutS. See also [[DNA Repair]] <br />
-
'''MLH1, MLH3, PMS1, PMS2''' are the human homologs of MutL<ref>PMID:15475387</ref> <br />
+
*'''MLH1, MLH3, PMS1, PMS2''' are the human homologs of MutL<ref>PMID:15475387</ref> <br />
== Disease ==
== Disease ==
Line 16: Line 16:
== Structural highlights ==
== Structural highlights ==
-
MutS is composed of several domains: N-terminal mismatch-recognition domain; connector domain; core domain; clamp domain; ATPase domain; helix-turn-helix domain. The complex between ''E. coli'' MutS and DNA in the scanning mode shows the straight DNA strand clamped between the two MutS monomers and held by the mismatch binding domain (residues 1-115) and the clamp domain (residues 444-503)<ref>PMID:33820992</ref>. In the 3D structure of the mismatch-bound MutS, the DNA strand is kinked by 60 degrees.
+
MutS is composed of several domains: N-terminal mismatch-recognition domain; connector domain; core domain; clamp domain; ATPase domain; helix-turn-helix domain. The complex between ''E. coli'' MutS and DNA in the scanning mode shows the straight DNA strand clamped between the two MutS monomers and held by the <scene name='91/916389/Cv/2'>mismatch binding domain</scene> (residues 1-115) and the <scene name='91/916389/Cv/3'>clamp domain</scene> (residues 444-503)<ref>PMID:33820992</ref>. In the 3D structure of the mismatch-bound MutS, the DNA strand is kinked by 60 degrees.
==3D structures of DNA mismatch repair protein==
==3D structures of DNA mismatch repair protein==

Current revision

E. coli MutS complex with DNA and ATP (PDB id 7ai5)

Drag the structure with the mouse to rotate

References

  1. Li GM. Mechanisms and functions of DNA mismatch repair. Cell Res. 2008 Jan;18(1):85-98. doi: 10.1038/cr.2007.115. PMID:18157157 doi:http://dx.doi.org/10.1038/cr.2007.115
  2. Lamers MH, Perrakis A, Enzlin JH, Winterwerp HH, de Wind N, Sixma TK. The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch. Nature. 2000 Oct 12;407(6805):711-7. PMID:11048711 doi:10.1038/35037523
  3. Guarne A, Ramon-Maiques S, Wolff EM, Ghirlando R, Hu X, Miller JH, Yang W. Structure of the MutL C-terminal domain: a model of intact MutL and its roles in mismatch repair. EMBO J. 2004 Oct 27;23(21):4134-45. Epub 2004 Oct 7. PMID:15470502
  4. Ellison AR, Lofing J, Bitter GA. Human MutL homolog (MLH1) function in DNA mismatch repair: a prospective screen for missense mutations in the ATPase domain. Nucleic Acids Res. 2004 Oct 8;32(18):5321-38. doi: 10.1093/nar/gkh855. Print, 2004. PMID:15475387 doi:http://dx.doi.org/10.1093/nar/gkh855
  5. Hsieh P, Yamane K. DNA mismatch repair: molecular mechanism, cancer, and ageing. Mech Ageing Dev. 2008 Jul-Aug;129(7-8):391-407. doi: 10.1016/j.mad.2008.02.012., Epub 2008 Mar 4. PMID:18406444 doi:http://dx.doi.org/10.1016/j.mad.2008.02.012
  6. Fernandez-Leiro R, Bhairosing-Kok D, Kunetsky V, Laffeber C, Winterwerp HH, Groothuizen F, Fish A, Lebbink JHG, Friedhoff P, Sixma TK, Lamers MH. The selection process of licensing a DNA mismatch for repair. Nat Struct Mol Biol. 2021 Apr;28(4):373-381. doi: 10.1038/s41594-021-00577-7., Epub 2021 Apr 5. PMID:33820992 doi:http://dx.doi.org/10.1038/s41594-021-00577-7

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

Personal tools