1ush

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[[Image:1ush.jpg|left|200px]]
 
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{{Structure
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==5'-NUCLEOTIDASE FROM E. COLI==
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|PDB= 1ush |SIZE=350|CAPTION= <scene name='initialview01'>1ush</scene>, resolution 1.73&Aring;
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<StructureSection load='1ush' size='340' side='right'caption='[[1ush]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
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|SITE= <scene name='pdbsite=ZNB:Zn+Binding+Site'>ZNB</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<table><tr><td colspan='2'>[[1ush]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1USH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1USH FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/5'-nucleotidase 5'-nucleotidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.5 3.1.3.5] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.73&#8491;</td></tr>
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|GENE= USHA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ush FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ush OCA], [https://pdbe.org/1ush PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ush RCSB], [https://www.ebi.ac.uk/pdbsum/1ush PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ush ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ush FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ush OCA], [http://www.ebi.ac.uk/pdbsum/1ush PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ush RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/USHA_ECOLI USHA_ECOLI] Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell.
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== Evolutionary Conservation ==
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'''5'-NUCLEOTIDASE FROM E. COLI'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/us/1ush_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/main_output.php?pdb_ID=1ush ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
The crystal structure of 5'-nucleotidase (5'-NT) from E. coli, also known as UDP-sugar hydrolase, has been determined at 1.7 A resolution. Two zinc ions are present in the active site, which is located in a cleft between two domains. The dimetal center and a catalytic Asp-His dyad are the main players in the catalytic mechanism. Structure-based sequence comparisons show that the structure also provides a model for animal 5'-NTs, which together with other ectonucleotidases terminate the action of nucleotides as extracellular signaling substances in the nervous system.
The crystal structure of 5'-nucleotidase (5'-NT) from E. coli, also known as UDP-sugar hydrolase, has been determined at 1.7 A resolution. Two zinc ions are present in the active site, which is located in a cleft between two domains. The dimetal center and a catalytic Asp-His dyad are the main players in the catalytic mechanism. Structure-based sequence comparisons show that the structure also provides a model for animal 5'-NTs, which together with other ectonucleotidases terminate the action of nucleotides as extracellular signaling substances in the nervous system.
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==About this Structure==
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X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site.,Knofel T, Strater N Nat Struct Biol. 1999 May;6(5):448-53. PMID:10331872<ref>PMID:10331872</ref>
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1USH is a [[Single protein]] structure of 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=1USH OCA].
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==Reference==
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X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site., Knofel T, Strater N, Nat Struct Biol. 1999 May;6(5):448-53. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10331872 10331872]
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[[Category: 5'-nucleotidase]]
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[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Knofel, T.]]
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[[Category: Strater, N.]]
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[[Category: hydrolase (phosphoric monoester)]]
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[[Category: periplasmic protein]]
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[[Category: phosphatase]]
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[[Category: udp-sugar hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:14:33 2008''
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ush" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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[[Category: Knofel T]]
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[[Category: Strater N]]

Current revision

5'-NUCLEOTIDASE FROM E. COLI

PDB ID 1ush

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OCA

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