1z5p: Difference between revisions

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[[Image:1z5p.png|left|200px]]


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==Crystal structure of MTA/AdoHcy nucleosidase with a ligand-free purine binding site==
The line below this paragraph, containing "STRUCTURE_1z5p", creates the "Structure Box" on the page.
<StructureSection load='1z5p' size='340' side='right'caption='[[1z5p]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1z5p]] is a 1 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=1Z5P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z5P FirstGlance]. <br>
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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]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=PE5:3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL'>PE5</scene></td></tr>
{{STRUCTURE_1z5p|  PDB=1z5p  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z5p OCA], [https://pdbe.org/1z5p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z5p RCSB], [https://www.ebi.ac.uk/pdbsum/1z5p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z5p ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MTNN_ECOLI MTNN_ECOLI] Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Can also use 5'-isobutylthioadenosine, 5'-n-butylthioadenosine, S-adenosyl-D-homocysteine, decarboxylated adenosylhomocysteine, deaminated adenosylhomocysteine and S-2-aza-adenosylhomocysteine as substrates.[HAMAP-Rule:MF_01684]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/z5/1z5p_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1z5p ConSurf].
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== Publication Abstract from PubMed ==
MTA/AdoHcy nucleosidase (MTAN) irreversibly hydrolyzes the N9-C1' bond in the nucleosides, 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (AdoHcy) to form adenine and the corresponding thioribose. MTAN plays a vital role in metabolic pathways involving methionine recycling, biological methylation, polyamine biosynthesis, and quorum sensing. Crystal structures of a wild-type (WT) MTAN complexed with glycerol, and mutant-enzyme and mutant-product complexes have been determined at 2.0A, 2.0A, and 2.1A resolution, respectively. The WT MTAN-glycerol structure provides a purine-free model and in combination with the previously solved thioribose-free MTAN-ADE structure, we now have separate apo structures for both MTAN binding subsites. The purine and thioribose-free states reveal an extensive enzyme-immobilized water network in their respective binding subsites. The Asp197Asn MTAN-MTA and Glu12Gln MTAN-MTR.ADE structures are the first enzyme-substrate and enzyme-product complexes reported for MTAN, respectively. These structures provide representative snapshots along the reaction coordinate and allow insight into the conformational changes of the enzyme and the nucleoside substrate. A "catalytic movie" detailing substrate binding, catalysis, and product release is presented.


===Crystal structure of MTA/AdoHcy nucleosidase with a ligand-free purine binding site===
Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis.,Lee JE, Smith GD, Horvatin C, Huang DJ, Cornell KA, Riscoe MK, Howell PL J Mol Biol. 2005 Sep 23;352(3):559-74. PMID:16109423<ref>PMID:16109423</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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(as it appears on PubMed at http://www.pubmed.gov), where 16109423 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_16109423}}
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</StructureSection>
==About this Structure==
[[1z5p]] is a 1 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=1Z5P OCA].
 
==Reference==
<ref group="xtra">PMID:016109423</ref><references group="xtra"/>
[[Category: Adenosylhomocysteine nucleosidase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Cornell, K A.]]
[[Category: Large Structures]]
[[Category: Horvatin, C.]]
[[Category: Cornell KA]]
[[Category: Howell, P L.]]
[[Category: Horvatin C]]
[[Category: Huang, D J.T.]]
[[Category: Howell PL]]
[[Category: Lee, J E.]]
[[Category: Huang DJT]]
[[Category: Riscoe, M K.]]
[[Category: Lee JE]]
[[Category: Smith, G D.]]
[[Category: Riscoe MK]]
[[Category: Hydrolase]]
[[Category: Smith GD]]
[[Category: Mixed alpha/beta]]