1svu
From Proteopedia
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|PDB= 1svu |SIZE=350|CAPTION= <scene name='initialview01'>1svu</scene>, resolution 2.66Å | |PDB= 1svu |SIZE=350|CAPTION= <scene name='initialview01'>1svu</scene>, resolution 2.66Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |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> |
| - | |ACTIVITY= [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] | + | |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> |
|GENE= HHAIM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=726 Haemophilus haemolyticus]) | |GENE= HHAIM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=726 Haemophilus haemolyticus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2hmy|2HMY]], [[1mht|1MHT]] | ||
| + | |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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[[Category: Zhang, X.]] | [[Category: Zhang, X.]] | ||
[[Category: Zhou, L.]] | [[Category: Zhou, L.]] | ||
| - | [[Category: SAH]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: UNX]] | ||
[[Category: dna methyltransferase]] | [[Category: dna methyltransferase]] | ||
[[Category: evolutionary link]] | [[Category: evolutionary link]] | ||
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[[Category: type i and ii restriction-modification system]] | [[Category: type i and ii restriction-modification system]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:47:42 2008'' |
Revision as of 20:47, 30 March 2008
| |||||||
| , resolution 2.66Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | HHAIM (Haemophilus haemolyticus) | ||||||
| Activity: | DNA (cytosine-5-)-methyltransferase, with EC number 2.1.1.37 | ||||||
| Related: | 2HMY, 1MHT
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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