1su1

<table><tr><td colspan='2'>[[1su1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SU1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SU1 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YFCE, B2300, C2843, Z3562, ECS3184 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1su1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1su1 OCA], [http://pdbe.org/1su1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1su1 RCSB], [http://www.ebi.ac.uk/pdbsum/1su1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1su1 ProSAT], [http://www.topsan.org/Proteins/MCSG/1su1 TOPSAN]</span></td></tr>

[[http://www.uniprot.org/uniprot/YFCE_ECOLI YFCE_ECOLI]] Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). The physiological substrate is unknown.

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== Publication Abstract from PubMed ==

Escherichia coli YfcE belongs to a conserved protein family within the calcineurin-like phosphoesterase superfamily (Pfam00149) that is widely distributed in bacteria and archaea. Superfamily members are metallophosphatases that include monoesterases and diesterases involved in a variety of cellular functions. YfcE exhibited catalytic activity against bis-p-nitrophenyl phosphate, a general substrate for phosphodiesterases, and had an absolute requirement for Mn2+. However, no activity was observed with phosphodiesters and over 50 naturally occurring phosphomonoesters. The crystal structure of the YfcE phosphodiesterase has been determined to 2.25 A resolution. YfcE has a beta-sandwich architecture similar to metallophosphatases of common ancestral origin. Unlike its more complex homologs that have added structural elements for regulation and substrate recognition, the relatively small 184-amino-acid protein has retained its ancestral simplicity. The tetrameric protein carries two zinc ions per active site from the E. coli extract that reflect the conserved di-Mn2+ active site geometry. A cocrystallized sulfate inhibitor mimics the binding of phosphate moeities in known ligand/phosphatase complexes. Thus, YfcE has a similar active site and biochemical mechanism as well-characterized superfamily members, while the YfcE phosphodiester-containing substrate is unique.

Structural and biochemical characterization of a novel Mn2+-dependent phosphodiesterase encoded by the yfcE gene.,Miller DJ, Shuvalova L, Evdokimova E, Savchenko A, Yakunin AF, Anderson WF Protein Sci. 2007 Jul;16(7):1338-48. doi: 10.1110/ps.072764907. PMID:17586769<ref>PMID:17586769</ref>

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

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== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Anderson, W F]]

[[Category: Evdokimova, E]]

[[Category: Structural genomic]]

[[Category: Miller, D J]]

[[Category: Savchenko, A]]

[[Category: Shuvalova, L]]

[[Category: Yakunin, A]]

[[Category: Yfce]]