1jys: Difference between revisions

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New page: left|200px<br /><applet load="1jys" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jys, resolution 1.90Å" /> '''Crystal Structure of...
 
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[[Image:1jys.gif|left|200px]]<br /><applet load="1jys" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Crystal Structure of E. coli MTA/AdoHcy Nucleosidase'''<br />


==Overview==
==Crystal Structure of E. coli MTA/AdoHcy Nucleosidase==
BACKGROUND: 5'-methylthioadenosine/S-adenosyl-homocysteine (MTA/AdoHcy), nucleosidase catalyzes the irreversible cleavage of 5'-methylthioadenosine, and S-adenosylhomocysteine to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. While this, enzyme is crucial for the metabolism of AdoHcy and MTA nucleosides in many, prokaryotic and lower eukaryotic organisms, it is absent in mammalian, cells. This metabolic difference represents an exploitable target for, rational drug design. RESULTS: The crystal structure of E. coli MTA/AdoHcy, nucleosidase was determined at 1.90 A resolution with the multiwavelength, anomalous diffraction (MAD) technique. Each monomer of the MTA/AdoHcy, nucleosidase dimer consists of a mixed alpha/beta domain with a, nine-stranded mixed beta sheet, flanked by six alpha helices and a small, 3(10) helix. Intersubunit contacts between the two monomers present in the, asymmetric unit are mediated primarily by helix-helix and helix-loop, hydrophobic interactions. The unexpected presence of an adenine molecule, in the active site of the enzyme has allowed the identification of both, substrate binding and potential catalytic amino acid residues., CONCLUSIONS: Although the sequence of E. coli MTA/AdoHcy nucleosidase has, almost no identity with any known enzyme, its tertiary structure is, similar to both the mammalian (trimeric) and prokaryotic (hexameric), purine nucleoside phosphorylases. The structure provides evidence that, this protein is functional as a dimer and that the dual specificity for, MTA and AdoHcy results from the truncation of a helix. The structure of, MTA/AdoHcy nucleosidase is the first structure of a prokaryotic nucleoside, N-ribohydrolase specific for 6-aminopurines.
<StructureSection load='1jys' size='340' side='right'caption='[[1jys]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1jys]] is a 2 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=1JYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JYS FirstGlance]. <br>
1JYS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ADE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Adenosylhomocysteine_nucleosidase Adenosylhomocysteine nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.9 3.2.2.9] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JYS OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jys OCA], [https://pdbe.org/1jys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jys RCSB], [https://www.ebi.ac.uk/pdbsum/1jys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jys ProSAT]</span></td></tr>
Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases., Lee JE, Cornell KA, Riscoe MK, Howell PL, Structure. 2001 Oct;9(10):941-53. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11591349 11591349]
</table>
[[Category: Adenosylhomocysteine nucleosidase]]
== 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>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jy/1jys_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=1jys ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Cornell, K.A.]]
[[Category: Cornell KA]]
[[Category: Howell, P.L.]]
[[Category: Howell PL]]
[[Category: Lee, J.E.]]
[[Category: Lee JE]]
[[Category: Riscoe, M.K.]]
[[Category: Riscoe MK]]
[[Category: ADE]]
[[Category: dimer]]
[[Category: mixed alpha/beta]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:41:45 2007''

Latest revision as of 10:42, 7 February 2024

Crystal Structure of E. coli MTA/AdoHcy NucleosidaseCrystal Structure of E. coli MTA/AdoHcy Nucleosidase

Structural highlights

1jys is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1jys, resolution 1.90Å

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