1u11

<StructureSection load='1u11' size='340' side='right' caption='[[1u11]], [[Resolution|resolution]] 1.55&Aring;' scene=''>

<table><tr><td colspan='2'>[[1u11]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acetobacter_aceti Acetobacter aceti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U11 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U11 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PurE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=435 Acetobacter aceti])</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=1u11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u11 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1u11 RCSB], [http://www.ebi.ac.uk/pdbsum/1u11 PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/Q2QJL3_ACEAC Q2QJL3_ACEAC]] Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR) (By similarity).[PIRNR:PIRNR001338]

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u1/1u11_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 crystal structure of Acetobacter aceti PurE was determined to a resolution of 1.55 A and is compared with the known structures of the class I PurEs from a mesophile, Escherichia coli, and a thermophile, Thermotoga maritima. Analyses of the general factors that increase protein stability are examined as potential explanations for the acid stability of A. aceti PurE. Increased inter-subunit hydrogen bonding and an increased number of arginine-containing salt bridges appear to account for the bulk of the increased acid stability. A chain of histidines linking two active sites is discussed in the context of the proton transfers catalyzed by the enzyme.

Acidophilic adaptations in the structure of Acetobacter aceti N5-carboxyaminoimidazole ribonucleotide mutase (PurE).,Settembre EC, Chittuluru JR, Mill CP, Kappock TJ, Ealick SE Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1753-60. Epub 2004, Sep 23. PMID:15388921<ref>PMID:15388921</ref>

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

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*[[Phosphoribosylaminoimidazole carboxylase|Phosphoribosylaminoimidazole carboxylase]]

[[Category: Chittuluru, J R]]

[[Category: Ealick, S E]]

[[Category: Kappock, T J]]

[[Category: Mill, C P]]

[[Category: Settembre, E C]]

[[Category: Acidophile]]

[[Category: Pure]]