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3jr5

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Revision as of 08:16, 1 November 2017

MutM lesion recognition control complex with N174C crosslinking site

Structural highlights

3jr5 is a 3 chain structure with sequence from Atcc 12980. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	3jr4
Activity:	DNA-(apurinic or apyrimidinic site) lyase, with EC number 4.2.99.18
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[P84131_GEOSE] Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates (By similarity).[HAMAP-Rule:MF_00103][SAAS:SAAS020629_004_120556]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

MutM, a bacterial DNA glycosylase, protects genome integrity by catalyzing glycosidic bond cleavage of 8-oxoguanine (oxoG) lesions, thereby initiating base excision DNA repair. The process of searching for and locating oxoG lesions is especially challenging, because of the close structural resemblance of oxoG to its million-fold more abundant progenitor, G. Extrusion of the target nucleobase from the DNA double helix to an extrahelical position is an essential step in lesion recognition and catalysis by MutM. Although the interactions between the extruded oxoG and the active site of MutM have been well characterized, little is known in structural detail regarding the interrogation of extruded normal DNA bases by MutM. Here we report the capture and structural elucidation of a complex in which MutM is attempting to present an undamaged G to its active site. The structure of this MutM-extrahelical G complex provides insights into the mechanism MutM employs to discriminate against extrahelical normal DNA bases and into the base extrusion process in general.

Entrapment and structure of an extrahelical guanine attempting to enter the active site of a bacterial DNA glycosylase, MutM.,Qi Y, Spong MC, Nam K, Karplus M, Verdine GL J Biol Chem. 2010 Jan 8;285(2):1468-78. Epub 2009 Nov 4. PMID:19889642^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Qi Y, Spong MC, Nam K, Karplus M, Verdine GL. Entrapment and structure of an extrahelical guanine attempting to enter the active site of a bacterial DNA glycosylase, MutM. J Biol Chem. 2010 Jan 8;285(2):1468-78. Epub 2009 Nov 4. PMID:19889642 doi:10.1074/jbc.M109.069799

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3jr5"

@@ Line 1: / Line 1: @@
 ==MutM lesion recognition control complex with N174C crosslinking site==
 <StructureSection load='3jr5' size='340' side='right' caption='[[3jr5]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3jr4|3jr4]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-(apurinic_or_apyrimidinic_site)_lyase DNA-(apurinic or apyrimidinic site) lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.99.18 4.2.99.18] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3jr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jr5 OCA], [http://pdbe.org/3jr5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jr5 RCSB], [http://www.ebi.ac.uk/pdbsum/3jr5 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3jr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jr5 OCA], [http://pdbe.org/3jr5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jr5 RCSB], [http://www.ebi.ac.uk/pdbsum/3jr5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jr5 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 30: / Line 31: @@
 </div>
 <div class="pdbe-citations 3jr5" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[DNA glycosylase|DNA glycosylase]]
 == References ==
 <references/>

3jr5

From Proteopedia

Revision as of 08:16, 1 November 2017

MutM lesion recognition control complex with N174C crosslinking site

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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