uu.seUppsala University Publications
Change search
ReferencesLink to record
Permanent link

Direct link
Structure of Escherichia coli ribose-5-phosphate isomerase: a ubiquitous enzyme of the pentose phosphate pathway and the Calvin cycle
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology.
Show others and affiliations
2003 (English)In: Structure, ISSN 0969-2126, E-ISSN 1878-4186, Vol. 11, no 1, 31-42 p.Article in journal (Refereed) Published
Abstract [en]

Ribose-5-phosphate isomerase A (RpiA; EC 5.3.1.6) interconverts ribose-5-phosphate and ribulose-5-phosphate. This enzyme plays essential roles in carbohydrate anabolism and catabolism; it is ubiquitous and highly conserved. The structure of RpiA from Escherichia coli was solved by multiwavelength anomalous diffraction (MAD) phasing, and refined to 1.5 A resolution (R factor 22.4%, R(free) 23.7%). RpiA exhibits an alpha/beta/(alpha/beta)/beta/alpha fold, some portions of which are similar to proteins of the alcohol dehydrogenase family. The two subunits of the dimer in the asymmetric unit have different conformations, representing the opening/closing of a cleft. Active site residues were identified in the cleft using sequence conservation, as well as the structure of a complex with the inhibitor arabinose-5-phosphate at 1.25 A resolution. A mechanism for acid-base catalysis is proposed.

Place, publisher, year, edition, pages
2003. Vol. 11, no 1, 31-42 p.
National Category
Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-293409DOI: 10.1016/S0969-2126(02)00933-4PubMedID: 12517338OAI: oai:DiVA.org:uu-293409DiVA: diva2:927669
Available from: 2016-05-12 Created: 2016-05-12 Last updated: 2016-05-12Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Mowbray, Sherry L
By organisation
Department of Cell and Molecular Biology
In the same journal
Structure
Cell and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 5 hits
ReferencesLink to record
Permanent link

Direct link