1ydx
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1ydx |SIZE=350|CAPTION= <scene name='initialview01'>1ydx</scene>, resolution 2.30Å | |PDB= 1ydx |SIZE=350|CAPTION= <scene name='initialview01'>1ydx</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ydx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ydx OCA], [http://www.ebi.ac.uk/pdbsum/1ydx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ydx RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Querol, E.]] | [[Category: Querol, E.]] | ||
[[Category: Quijada, O.]] | [[Category: Quijada, O.]] | ||
| - | [[Category: CL]] | ||
[[Category: type-i hsd]] | [[Category: type-i hsd]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:04:16 2008'' |
Revision as of 22:04, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Type-I restriction-modification system S subunit from M. genitalium
Overview
The crystal structure of the eubacteria Mycoplasma genitalium ORF MG438 polypeptide, determined by multiple anomalous dispersion and refined at 2.3 A resolution, reveals the organization of S subunits from the Type I restriction and modification system. The structure consists of two globular domains, with about 150 residues each, separated by a pair of 40 residue long antiparallel alpha-helices. The globular domains correspond to the variable target recognition domains (TRDs), as previously defined for S subunits on sequence analysis, while the two helices correspond to the central (CR1) and C-terminal (CR2) conserved regions, respectively. The structure of the MG438 subunit presents an overall cyclic topology with an intramolecular 2-fold axis that superimposes the N and the C-half parts, each half containing a globular domain and a conserved helix. TRDs are found to be structurally related with the small domain of the Type II N6-adenine DNA MTase TaqI. These relationships together with the structural peculiarities of MG438, in particular the presence of the intramolecular quasi-symmetry, allow the proposal of a model for S subunits recognition of their DNA targets in agreement with previous experimental results. In the crystal, two subunits of MG438 related by a crystallographic 2-fold axis present a large contact area mainly involving the symmetric interactions of a cluster of exposed hydrophobic residues. Comparison with the recently reported structure of an S subunit from the archaea Methanococcus jannaschii highlights the structural features preserved despite a sequence identity below 20%, but also reveals important differences in the globular domains and in their disposition with respect to the conserved regions.
About this Structure
1YDX is a Single protein structure of sequence from Mycoplasma genitalium. Full crystallographic information is available from OCA.
Reference
Crystal structure of a putative type I restriction-modification S subunit from Mycoplasma genitalium., Calisto BM, Pich OQ, Pinol J, Fita I, Querol E, Carpena X, J Mol Biol. 2005 Aug 26;351(4):749-62. PMID:16038930
Page seeded by OCA on Mon Mar 31 01:04:16 2008
