1svu

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[[Image:1svu.gif|left|200px]]
[[Image:1svu.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1svu |SIZE=350|CAPTION= <scene name='initialview01'>1svu</scene>, resolution 2.66&Aring;
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The line below this paragraph, containing "STRUCTURE_1svu", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= HHAIM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=726 Haemophilus haemolyticus])
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-->
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|DOMAIN=
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{{STRUCTURE_1svu| PDB=1svu | SCENE= }}
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|RELATEDENTRY=[[2hmy|2HMY]], [[1mht|1MHT]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1svu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svu OCA], [http://www.ebi.ac.uk/pdbsum/1svu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1svu RCSB]</span>
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}}
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'''Structure of the Q237W mutant of HhaI DNA methyltransferase: an insight into protein-protein interactions'''
'''Structure of the Q237W mutant of HhaI DNA methyltransferase: an insight into protein-protein interactions'''
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/15195996 15195996]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15195996 15195996]
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[[Category: DNA (cytosine-5-)-methyltransferase]]
 
[[Category: Haemophilus haemolyticus]]
[[Category: Haemophilus haemolyticus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Zhang, X.]]
[[Category: Zhang, X.]]
[[Category: Zhou, L.]]
[[Category: Zhou, L.]]
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[[Category: dna methyltransferase]]
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[[Category: Dna methyltransferase]]
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[[Category: evolutionary link]]
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[[Category: Evolutionary link]]
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[[Category: protein-protein interaction]]
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[[Category: Protein-protein interaction]]
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[[Category: type i and ii restriction-modification system]]
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[[Category: Type i and ii restriction-modification system]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:11:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:47:42 2008''
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Revision as of 06:11, 3 May 2008

Template:STRUCTURE 1svu

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. 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 Sat May 3 09:11:46 2008

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