1svu
From Proteopedia
(New page: 200px<br /><applet load="1svu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1svu, resolution 2.66Å" /> '''Structure of the Q23...) |
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| - | [[Image:1svu.gif|left|200px]]<br /><applet load="1svu" size=" | + | [[Image:1svu.gif|left|200px]]<br /><applet load="1svu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1svu, resolution 2.66Å" /> | caption="1svu, resolution 2.66Å" /> | ||
'''Structure of the Q237W mutant of HhaI DNA methyltransferase: an insight into protein-protein interactions'''<br /> | '''Structure of the Q237W mutant of HhaI DNA methyltransferase: an insight into protein-protein interactions'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined the structure of a mutant (Q237W) of HhaI DNA | + | We have determined the structure of a mutant (Q237W) of HhaI DNA methyltransferase, complexed with the methyl-donor product AdoHcy. The Q237W mutant proteins were crystallized in the monoclinic space group C2 with two molecules in the crystallographic asymmetric unit. Protein-protein interface calculations in the crystal lattices suggest that the dimer interface has the specific characteristics for homodimer protein-protein interactions, while the two active sites are spatially independent on the outer surface of the dimer. The solution behavior suggests the formation of HhaI dimers as well. The same HhaI dimer interface is also observed in the previously characterized binary (M.HhaI-AdoMet) and ternary (M.HhaI-DNA-AdoHcy) complex structures, crystallized in different space groups. The dimer is characterized either by a non-crystallographic two-fold symmetry or a crystallographic symmetry. The dimer interface involves three segments: the amino-terminal residues 2-8, the carboxy-terminal residues 313-327, and the linker (amino acids 179-184) between the two functional domains--the catalytic methylation domain and the DNA target recognition domain. Both the amino- and carboxy-terminal segments are part of the methylation domain. We also examined protein-protein interactions of other structurally characterized DNA MTases, which are often found as a 2-fold related 'dimer' with the largest dimer interface area for the group-beta MTases. A possible evolutionary link between the Type I and Type II restriction-modification systems is discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1SVU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_haemolyticus Haemophilus haemolyticus] with SO4, SAH and UNX as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA_(cytosine-5-)-methyltransferase DNA (cytosine-5-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.37 2.1.1.37] Full crystallographic information is available from [http:// | + | 1SVU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_haemolyticus Haemophilus haemolyticus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=SAH:'>SAH</scene> and <scene name='pdbligand=UNX:'>UNX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA_(cytosine-5-)-methyltransferase DNA (cytosine-5-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.37 2.1.1.37] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Cheng, X.]] | [[Category: Cheng, X.]] | ||
[[Category: Dong, A.]] | [[Category: Dong, A.]] | ||
| - | [[Category: Roberts, R | + | [[Category: Roberts, R J.]] |
[[Category: Stickel, S.]] | [[Category: Stickel, S.]] | ||
[[Category: Zhang, X.]] | [[Category: Zhang, X.]] | ||
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[[Category: type i and ii restriction-modification systems]] | [[Category: type i and ii restriction-modification systems]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:43 2008'' |
Revision as of 13:05, 21 February 2008
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Structure of the Q237W mutant of HhaI DNA methyltransferase: an insight into protein-protein interactions
Overview
We have determined the structure of a mutant (Q237W) of HhaI DNA methyltransferase, complexed with the methyl-donor product AdoHcy. The Q237W mutant proteins were crystallized in the monoclinic space group C2 with two molecules in the crystallographic asymmetric unit. Protein-protein interface calculations in the crystal lattices suggest that the dimer interface has the specific characteristics for homodimer protein-protein interactions, while the two active sites are spatially independent on the outer surface of the dimer. The solution behavior suggests the formation of HhaI dimers as well. The same HhaI dimer interface is also observed in the previously characterized binary (M.HhaI-AdoMet) and ternary (M.HhaI-DNA-AdoHcy) complex structures, crystallized in different space groups. The dimer is characterized either by a non-crystallographic two-fold symmetry or a crystallographic symmetry. The dimer interface involves three segments: the amino-terminal residues 2-8, the carboxy-terminal residues 313-327, and the linker (amino acids 179-184) between the two functional domains--the catalytic methylation domain and the DNA target recognition domain. Both the amino- and carboxy-terminal segments are part of the methylation domain. We also examined protein-protein interactions of other structurally characterized DNA MTases, which are often found as a 2-fold related 'dimer' with the largest dimer interface area for the group-beta MTases. A possible evolutionary link between the Type I and Type II restriction-modification systems is discussed.
About this Structure
1SVU is a Single protein structure of sequence from Haemophilus haemolyticus with , and as ligands. Active as DNA (cytosine-5-)-methyltransferase, with EC number 2.1.1.37 Full crystallographic information is available from OCA.
Reference
Structure of the Q237W mutant of HhaI DNA methyltransferase: an insight into protein-protein interactions., Dong A, Zhou L, Zhang X, Stickel S, Roberts RJ, Cheng X, Biol Chem. 2004 May;385(5):373-9. PMID:15195996
Page seeded by OCA on Thu Feb 21 15:05:43 2008
Categories: DNA (cytosine-5-)-methyltransferase | Haemophilus haemolyticus | Single protein | Cheng, X. | Dong, A. | Roberts, R J. | Stickel, S. | Zhang, X. | Zhou, L. | SAH | SO4 | UNX | Dna methyltransferase | Evolutionary link | Protein-protein interactions | Type i and ii restriction-modification systems
