1nn4: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1nn4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NN4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NN4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1nn4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NN4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NN4 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPIB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPIB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribose-5-phosphate_isomerase Ribose-5-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.6 5.3.1.6] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribose-5-phosphate_isomerase Ribose-5-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.6 5.3.1.6] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nn4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nn4 RCSB], [http://www.ebi.ac.uk/pdbsum/1nn4 PDBsum], [http://www.topsan.org/Proteins/MCSG/1nn4 TOPSAN]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nn4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nn4 RCSB], [http://www.ebi.ac.uk/pdbsum/1nn4 PDBsum], [http://www.topsan.org/Proteins/MCSG/1nn4 TOPSAN]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/RPIB_ECOLI RPIB_ECOLI]] In addition to its activity on D-ribose 5-phosphate it probably also has activity on D-allose 6-phosphate.<ref>PMID:8576032</ref> <ref>PMID:4909663</ref> <ref>PMID:1104357</ref> <ref>PMID:9401019</ref> <ref>PMID:18640127</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Ribose-5-phosphate isomerase]] | [[Category: Ribose-5-phosphate isomerase]] | ||
[[Category: Andersson, C E | [[Category: Andersson, C E]] | ||
[[Category: Arrowsmith, C | [[Category: Arrowsmith, C]] | ||
[[Category: Beasley, S L | [[Category: Beasley, S L]] | ||
[[Category: Edwards, A M | [[Category: Edwards, A M]] | ||
[[Category: Evdokimova, E | [[Category: Evdokimova, E]] | ||
[[Category: Joachimiak, A | [[Category: Joachimiak, A]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Mowbray, S L | [[Category: Mowbray, S L]] | ||
[[Category: Savchenko, A | [[Category: Savchenko, A]] | ||
[[Category: Skarina, T | [[Category: Skarina, T]] | ||
[[Category: Zhang, R G | [[Category: Zhang, R G]] | ||
[[Category: Alpha/beta/alpha sandwich]] | [[Category: Alpha/beta/alpha sandwich]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Mcsg]] | [[Category: Mcsg]] | ||
[[Category: | [[Category: PSI, Protein structure initiative]] | ||
Revision as of 04:46, 25 December 2014
Structural Genomics, RpiB/AlsBStructural Genomics, RpiB/AlsB
Structural highlights
Function[RPIB_ECOLI] In addition to its activity on D-ribose 5-phosphate it probably also has activity on D-allose 6-phosphate.[1] [2] [3] [4] [5] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedRibose-5-phosphate isomerases (EC 5.3.1.6) interconvert ribose 5-phosphate and ribulose 5-phosphate. This reaction permits the synthesis of ribose from other sugars, as well as the recycling of sugars from nucleotide breakdown. Two unrelated types of enzyme can catalyze the reaction. The most common, RpiA, is present in almost all organisms (including Escherichia coli), and is highly conserved. The second type, RpiB, is present in some bacterial and eukaryotic species and is well conserved. In E.coli, RpiB is sometimes referred to as AlsB, because it can take part in the metabolism of the rare sugar, allose, as well as the much more common ribose sugars. We report here the structure of RpiB/AlsB from E.coli, solved by multi-wavelength anomalous diffraction (MAD) phasing, and refined to 2.2A resolution. RpiB is the first structure to be solved from pfam02502 (the RpiB/LacAB family). It exhibits a Rossmann-type alphabetaalpha-sandwich fold that is common to many nucleotide-binding proteins, as well as other proteins with different functions. This structure is quite distinct from that of the previously solved RpiA; although both are, to some extent, based on the Rossmann fold, their tertiary and quaternary structures are very different. The four molecules in the RpiB asymmetric unit represent a dimer of dimers. Active-site residues were identified at the interface between the subunits, such that each active site has contributions from both subunits. Kinetic studies indicate that RpiB is nearly as efficient as RpiA, despite its completely different catalytic machinery. The sequence and structural results further suggest that the two homologous components of LacAB (galactose-6-phosphate isomerase) will compose a bi-functional enzyme; the second activity is unknown. The 2.2 A resolution structure of RpiB/AlsB from Escherichia coli illustrates a new approach to the ribose-5-phosphate isomerase reaction.,Zhang RG, Andersson CE, Skarina T, Evdokimova E, Edwards AM, Joachimiak A, Savchenko A, Mowbray SL J Mol Biol. 2003 Oct 3;332(5):1083-94. PMID:14499611[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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