Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/111084
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Campo DC | Valor | Lengua/Idioma |
---|---|---|
dc.contributor.author | Calisto, Bárbara M. | - |
dc.contributor.author | Pich, Oscar Q. | - |
dc.contributor.author | Piñol, Jaume | - |
dc.contributor.author | Fita, Ignacio | - |
dc.contributor.author | Querol, Enrique | - |
dc.contributor.author | Carpena, Xavi | - |
dc.date.accessioned | 2015-02-24T08:40:43Z | - |
dc.date.available | 2015-02-24T08:40:43Z | - |
dc.date.issued | 2005-08-26 | - |
dc.identifier | doi: 10.1016/j.jmb.2005.06.050 | - |
dc.identifier | issn: 0022-2836 | - |
dc.identifier.citation | Journal of Molecular Biology 351(4): 749-762 (2005) | - |
dc.identifier.uri | http://hdl.handle.net/10261/111084 | - |
dc.description.abstract | The crystal structure of the eubacteria Mycoplasma genitalium ORF MG438 polypeptide, determined by multiple anomalous dispersion and refined at 2.3 Å 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 α-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. | - |
dc.description.sponsorship | This work was supported by grants BIO2002-04419 and BFU2004-06377-C02-01 to I.F. and E.Q., respectively. O.Q. acknowledges a predoctoral fellowship from CeRBa (Centre de Referència en Biotecnologia) | - |
dc.publisher | Academic Press | - |
dc.rights | closedAccess | - |
dc.subject | Crystal structures | - |
dc.subject | Type I restriction and modification system | - |
dc.subject | HsdS | - |
dc.subject | Mycoplasma genitalium | - |
dc.subject | DNA recognition | - |
dc.title | Crystal structure of a putative type I restriction-modification S subunit from Mycoplasma genitalium | - |
dc.type | artículo | - |
dc.identifier.doi | 10.1016/j.jmb.2005.06.050 | - |
dc.relation.publisherversion | http://dx.doi.org/10.1016/j.jmb.2005.06.050 | - |
dc.date.updated | 2015-02-24T08:40:43Z | - |
dc.description.version | Peer Reviewed | - |
dc.language.rfc3066 | eng | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairetype | artículo | - |
item.fulltext | No Fulltext | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.cerifentitytype | Publications | - |
item.grantfulltext | none | - |
Aparece en las colecciones: | (IBMB) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
43
checked on 08-may-2024
WEB OF SCIENCETM
Citations
42
checked on 28-feb-2024
Page view(s)
362
checked on 13-may-2024
Download(s)
124
checked on 13-may-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.