1z5o

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[[Image:1z5o.gif|left|200px]]<br /><applet load="1z5o" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1z5o.gif|left|200px]]
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caption="1z5o, resolution 2.00&Aring;" />
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'''Crystal structure of MTA/AdoHcy nucleosidase Asp197Asn mutant complexed with 5'-methylthioadenosine'''<br />
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{{Structure
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|PDB= 1z5o |SIZE=350|CAPTION= <scene name='initialview01'>1z5o</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MTA:5'-DEOXY-5'-METHYLTHIOADENOSINE'>MTA</scene>
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|ACTIVITY= [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]
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|GENE= mtnN, mtn, pfs ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Crystal structure of MTA/AdoHcy nucleosidase Asp197Asn mutant complexed with 5'-methylthioadenosine'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1Z5O 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 <scene name='pdbligand=MTA:'>MTA</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z5O OCA].
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1Z5O 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=1Z5O OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16109423 16109423]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16109423 16109423]
[[Category: Adenosylhomocysteine nucleosidase]]
[[Category: Adenosylhomocysteine nucleosidase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: mixed alpha/beta]]
[[Category: mixed alpha/beta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:31:29 2008''

Revision as of 13:31, 20 March 2008


PDB ID 1z5o

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands:
Gene: mtnN, mtn, pfs (Escherichia coli)
Activity: Adenosylhomocysteine nucleosidase, with EC number 3.2.2.9
Coordinates: save as pdb, mmCIF, xml



Crystal structure of MTA/AdoHcy nucleosidase Asp197Asn mutant complexed with 5'-methylthioadenosine


Overview

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.

About this Structure

1Z5O is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

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