4gij: Difference between revisions

<StructureSection load='4gij' size='340' side='right' caption='[[4gij]], [[Resolution|resolution]] 1.94&Aring;' scene=''>

<table><tr><td colspan='2'>[[4gij]] is a 3 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=4GIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GIJ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gik|4gik]], [[4gil|4gil]], [[4gim|4gim]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b2165, JW2152, psuG, yeiN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=4gij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gij OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gij RCSB], [http://www.ebi.ac.uk/pdbsum/4gij PDBsum]</span></td></tr>

== Publication Abstract from PubMed ==

Pseudouridine (Psi), the most abundant modification in RNA, is synthesized in situ using Psi synthase. Recently, a pathway for the degradation of Psi was described [Preumont, A., Snoussi, K., Stroobant, V., Collet, J. F., and Van Schaftingen, E. (2008) J. Biol. Chem. 283, 25238-25246]. In this pathway, Psi is first converted to Psi 5'-monophosphate (PsiMP) by Psi kinase and then PsiMP is degraded by PsiMP glycosidase to uracil and ribose 5-phosphate. PsiMP glycosidase is the first example of a mechanistically characterized enzyme that cleaves a C-C glycosidic bond. Here we report X-ray crystal structures of Escherichia coli PsiMP glycosidase and a complex of the K166A mutant with PsiMP. We also report the structures of a ring-opened ribose 5-phosphate adduct and a ring-opened ribose PsiMP adduct. These structures provide four snapshots along the reaction coordinate. The structural studies suggested that the reaction utilizes a Lys166 adduct during catalysis. Biochemical and mass spectrometry data further confirmed the existence of a lysine adduct. We used site-directed mutagenesis combined with kinetic analysis to identify roles for specific active site residues. Together, these data suggest that PsiMP glycosidase catalyzes the cleavage of the C-C glycosidic bond through a novel ribose ring-opening mechanism.

 

Pseudouridine monophosphate glycosidase: a new glycosidase mechanism.,Huang S, Mahanta N, Begley TP, Ealick SE Biochemistry. 2012 Nov 13;51(45):9245-55. doi: 10.1021/bi3006829. Epub 2012 Oct, 30. PMID:23066817<ref>PMID:23066817</ref>

 

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

[[Category: Begley, T P]]

[[Category: Ealick, S E]]

[[Category: Huang, S]]

[[Category: Mahanta, N]]

[[Category: Alpha-beta-alpha sandwich fold]]

[[Category: Hydrolase]]