Publication
High-resolution structure of an atypical α-phosphoglucomutase related to eukaryotic phosphomannomutases
| dc.contributor.author | Nogly, Przemyslaw | |
| dc.contributor.author | Matias, Pedro M. | |
| dc.contributor.author | de Rosa, Matteo | |
| dc.contributor.author | Castro, Rute | |
| dc.contributor.author | Santos, Helena | |
| dc.contributor.author | Neves, Ana Rute | |
| dc.contributor.author | Archer, Margarida | |
| dc.date.accessioned | 2015-11-04T10:51:13Z | |
| dc.date.available | 2015-11-04T10:51:13Z | |
| dc.date.issued | 2013-10 | |
| dc.description.abstract | The first structure of a bacterial α-phosphoglucomutase with an overall fold similar to eukaryotic phosphomannomutases is reported. Unlike most α-phosphoglucomutases within the α-D-phosphohexomutase superfamily, it belongs to subclass IIb of the haloacid dehalogenase superfamily (HADSF). It catalyzes the reversible conversion of α-glucose 1-phosphate to glucose 6-phosphate. The crystal structure of α-phosphoglucomutase from Lactococcus lactis (APGM) was determined at 1.5 Å resolution and contains a sulfate and a glycerol bound at the enzyme active site that partially mimic the substrate. A dimeric form of APGM is present in the crystal and in solution, an arrangement that may be functionally relevant. The catalytic mechanism of APGM and its strict specificity towards α-glucose 1-phosphate are discussed. | pt_PT |
| dc.description.sponsorship | Diamond Light Source. | pt_PT |
| dc.identifier | 10.1107/S0907444913017046 | |
| dc.identifier.doi | 10.1107/S0907444913017046 | |
| dc.identifier.uri | http://hdl.handle.net/10400.7/468 | |
| dc.language.iso | eng | pt_PT |
| dc.peerreviewed | yes | pt_PT |
| dc.publisher | Wiley-Blackwell | pt_PT |
| dc.relation | Structural Biology of Membrane Proteins | |
| dc.relation.publisherversion | http://journals.iucr.org/d/issues/2013/10/00/dz5291/index.html | pt_PT |
| dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | pt_PT |
| dc.subject | α-phosphoglucomutases | pt_PT |
| dc.subject | haloacid dehalogenase superfamily | pt_PT |
| dc.subject | Lactococcus lactis | pt_PT |
| dc.subject | phosphomannomutases | pt_PT |
| dc.subject | α-glucose 1-phosphate | pt_PT |
| dc.subject | eukaryotic phosphomannomutases | pt_PT |
| dc.subject | sugar metabolism | pt_PT |
| dc.title | High-resolution structure of an atypical α-phosphoglucomutase related to eukaryotic phosphomannomutases | pt_PT |
| dc.type | journal article | |
| dspace.entity.type | Publication | |
| oaire.awardTitle | Structural Biology of Membrane Proteins | |
| oaire.awardURI | info:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-MIC%2F099963%2F2008/PT | |
| oaire.awardURI | info:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-PRO%2F103718%2F2008/PT | |
| oaire.awardURI | info:eu-repo/grantAgreement/EC/FP7/211800/EU | |
| oaire.citation.endPage | 2016 | pt_PT |
| oaire.citation.issue | 10 | pt_PT |
| oaire.citation.startPage | 2008 | pt_PT |
| oaire.citation.title | Acta Crystallographica Section D-Biological Crystallography | pt_PT |
| oaire.citation.volume | 69 | pt_PT |
| oaire.fundingStream | 3599-PPCDT | |
| oaire.fundingStream | 3599-PPCDT | |
| oaire.fundingStream | FP7 | |
| project.funder.identifier | http://doi.org/10.13039/501100001871 | |
| project.funder.identifier | http://doi.org/10.13039/501100001871 | |
| project.funder.identifier | http://doi.org/10.13039/501100008530 | |
| project.funder.name | Fundação para a Ciência e a Tecnologia | |
| project.funder.name | Fundação para a Ciência e a Tecnologia | |
| project.funder.name | European Commission | |
| rcaap.rights | openAccess | pt_PT |
| rcaap.type | article | pt_PT |
| relation.isProjectOfPublication | e1524449-b5b2-4863-93c7-1f319ebe3ff6 | |
| relation.isProjectOfPublication | 98c4a4f5-9047-4e16-bf57-37a57741becb | |
| relation.isProjectOfPublication | 9a287bd0-ed06-4274-b6de-b3daa5054ae3 | |
| relation.isProjectOfPublication.latestForDiscovery | 9a287bd0-ed06-4274-b6de-b3daa5054ae3 |