1t8w: Difference between revisions

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New page: left|200px<br /><applet load="1t8w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t8w, resolution 2.80Å" /> '''Crystal Structure of...
 
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[[Image:1t8w.jpg|left|200px]]<br /><applet load="1t8w" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1t8w, resolution 2.80&Aring;" />
'''Crystal Structure of E. coli AMP Nucleosidase'''<br />


==Overview==
==Crystal Structure of E. coli AMP Nucleosidase==
AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to form adenine and, ribose 5-phosphate. The enzyme is found only in prokaryotes, where it, plays a role in purine nucleoside salvage and intracellular AMP level, regulation. Enzyme activity is stimulated by ATP and suppressed by, phosphate. The structure of unliganded AMN was determined at 2.7 A, resolution, and structures of the complexes with either formycin, 5'-monophosphate or inorganic phosphate were determined at 2.6 A and 3.0 A, resolution, respectively. AMN is a biological homohexamer, and each, monomer is composed of two domains: a catalytic domain and a putative, regulatory domain. The overall topology of the catalytic domain and some, features of the substrate binding site resemble those of the nucleoside, phosphorylases, demonstrating that AMN is a new member of the family. The, structure of the regulatory domain consists of a long helix and a, four-stranded sheet and has a novel topology.
<StructureSection load='1t8w' size='340' side='right'caption='[[1t8w]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1t8w]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T8W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T8W FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t8w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t8w OCA], [https://pdbe.org/1t8w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t8w RCSB], [https://www.ebi.ac.uk/pdbsum/1t8w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t8w ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMN_ECOLI AMN_ECOLI] Involved in regulation of AMP concentrations.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t8/1t8w_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1t8w ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to form adenine and ribose 5-phosphate. The enzyme is found only in prokaryotes, where it plays a role in purine nucleoside salvage and intracellular AMP level regulation. Enzyme activity is stimulated by ATP and suppressed by phosphate. The structure of unliganded AMN was determined at 2.7 A resolution, and structures of the complexes with either formycin 5'-monophosphate or inorganic phosphate were determined at 2.6 A and 3.0 A resolution, respectively. AMN is a biological homohexamer, and each monomer is composed of two domains: a catalytic domain and a putative regulatory domain. The overall topology of the catalytic domain and some features of the substrate binding site resemble those of the nucleoside phosphorylases, demonstrating that AMN is a new member of the family. The structure of the regulatory domain consists of a long helix and a four-stranded sheet and has a novel topology.


==About this Structure==
Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases.,Zhang Y, Cottet SE, Ealick SE Structure. 2004 Aug;12(8):1383-94. PMID:15296732<ref>PMID:15296732</ref>
1T8W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/AMP_nucleosidase AMP nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.4 3.2.2.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T8W OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases., Zhang Y, Cottet SE, Ealick SE, Structure. 2004 Aug;12(8):1383-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15296732 15296732]
</div>
[[Category: AMP nucleosidase]]
<div class="pdbe-citations 1t8w" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Cottet, S.E.]]
[[Category: Cottet SE]]
[[Category: Ealick, S.E.]]
[[Category: Ealick SE]]
[[Category: Zhang, Y.]]
[[Category: Zhang Y]]
[[Category: alpha-beta fold]]
[[Category: alpha-beta-alpha sandwich]]
 
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