1lx7

<StructureSection load='1lx7' size='340' side='right' caption='[[1lx7]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[1lx7]] is a 2 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=1LX7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LX7 FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1k3f|1k3f]]</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uridine_phosphorylase Uridine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.3 2.4.2.3] </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=1lx7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lx7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lx7 RCSB], [http://www.ebi.ac.uk/pdbsum/1lx7 PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/1lx7 TOPSAN]</span></td></tr>

[[http://www.uniprot.org/uniprot/UDP_ECOLI UDP_ECOLI]] Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lx/1lx7_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

The 2.0 A crystal structure has been determined for Escherichia coli uridine phosphorylase (UP), an essential enzyme in nucleotide biosynthesis that catalyzes the phosphorolytic cleavage of the C-N glycosidic bond of uridine to ribose-1-phosphate and uracil. The structure determination of two independent monomers in the asymmetric unit revealed the residue composition and atomic details of the apo configurations of each active site. The native hexameric UP enzyme was revealed by applying threefold crystallographic symmetry to the contents of the asymmetric unit. The 2.0 A model reveals a closer structural relationship to other nucleotide phosphorylase enzymes than was previously appreciated.

Structure of Escherichia coli uridine phosphorylase at 2.0 A.,Burling FT, Kniewel R, Buglino JA, Chadha T, Beckwith A, Lima CD Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):73-6. Epub 2002 Dec, 19. PMID:12499542<ref>PMID:12499542</ref>

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

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*[[Uridine phosphorylase|Uridine phosphorylase]]

[[Category: Uridine phosphorylase]]

[[Category: Beckwith, A]]

[[Category: Buglino, J A]]

[[Category: Burley, S K]]

[[Category: Burling, T]]

[[Category: Chadna, T]]

[[Category: Kniewel, R]]

[[Category: Lima, C D]]

[[Category: Udrpase]]