1ee8
From Proteopedia
(New page: 200px<br /><applet load="1ee8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ee8, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1ee8.gif|left|200px]]<br /><applet load="1ee8" size=" | + | [[Image:1ee8.gif|left|200px]]<br /><applet load="1ee8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ee8, resolution 1.9Å" /> | caption="1ee8, resolution 1.9Å" /> | ||
'''CRYSTAL STRUCTURE OF MUTM (FPG) PROTEIN FROM THERMUS THERMOPHILUS HB8'''<br /> | '''CRYSTAL STRUCTURE OF MUTM (FPG) PROTEIN FROM THERMUS THERMOPHILUS HB8'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The MutM [formamidopyrimidine DNA glycosylase (Fpg)] protein is a | + | The MutM [formamidopyrimidine DNA glycosylase (Fpg)] protein is a trifunctional DNA base excision repair enzyme that removes a wide range of oxidatively damaged bases (N-glycosylase activity) and cleaves both the 3'- and 5'-phosphodiester bonds of the resulting apurinic/apyrimidinic site (AP lyase activity). The crystal structure of MutM from an extreme thermophile, Thermus thermophilus HB8, was determined at 1.9 A resolution with multiwavelength anomalous diffraction phasing using the intrinsic Zn(2+) ion of the zinc finger. MutM is composed of two distinct and novel domains connected by a flexible hinge. There is a large, electrostatically positive cleft lined by highly conserved residues between the domains. On the basis of the three-dimensional structure and taking account of previous biochemical experiments, we propose a DNA-binding mode and reaction mechanism for MutM. The locations of the putative catalytic residues and the two DNA-binding motifs (the zinc finger and the helix-two-turns-helix motifs) suggest that the oxidized base is flipped out from double-stranded DNA in the binding mode and excised by a catalytic mechanism similar to that of bifunctional base excision repair enzymes. |
==About this Structure== | ==About this Structure== | ||
| - | 1EE8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1EE8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EE8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Kuramitsu, S.]] | [[Category: Kuramitsu, S.]] | ||
[[Category: Mikawa, T.]] | [[Category: Mikawa, T.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Sugahara, M.]] | [[Category: Sugahara, M.]] | ||
[[Category: Yamamoto, M.]] | [[Category: Yamamoto, M.]] | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:26:48 2008'' |
Revision as of 10:26, 21 February 2008
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CRYSTAL STRUCTURE OF MUTM (FPG) PROTEIN FROM THERMUS THERMOPHILUS HB8
Overview
The MutM [formamidopyrimidine DNA glycosylase (Fpg)] protein is a trifunctional DNA base excision repair enzyme that removes a wide range of oxidatively damaged bases (N-glycosylase activity) and cleaves both the 3'- and 5'-phosphodiester bonds of the resulting apurinic/apyrimidinic site (AP lyase activity). The crystal structure of MutM from an extreme thermophile, Thermus thermophilus HB8, was determined at 1.9 A resolution with multiwavelength anomalous diffraction phasing using the intrinsic Zn(2+) ion of the zinc finger. MutM is composed of two distinct and novel domains connected by a flexible hinge. There is a large, electrostatically positive cleft lined by highly conserved residues between the domains. On the basis of the three-dimensional structure and taking account of previous biochemical experiments, we propose a DNA-binding mode and reaction mechanism for MutM. The locations of the putative catalytic residues and the two DNA-binding motifs (the zinc finger and the helix-two-turns-helix motifs) suggest that the oxidized base is flipped out from double-stranded DNA in the binding mode and excised by a catalytic mechanism similar to that of bifunctional base excision repair enzymes.
About this Structure
1EE8 is a Single protein structure of sequence from Thermus thermophilus with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8., Sugahara M, Mikawa T, Kumasaka T, Yamamoto M, Kato R, Fukuyama K, Inoue Y, Kuramitsu S, EMBO J. 2000 Aug 1;19(15):3857-69. PMID:10921868
Page seeded by OCA on Thu Feb 21 12:26:48 2008
Categories: Single protein | Thermus thermophilus | Fukuyama, K. | Inoue, Y. | Kato, R. | Kumasaka, T. | Kuramitsu, S. | Mikawa, T. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sugahara, M. | Yamamoto, M. | ZN | Beta sandwich | Helix two-turns helix | Riken structural genomics/proteomics initiative | Rsgi | Structural genomics | Zinc finger
