1z5o
From Proteopedia
(New page: 200px<br /><applet load="1z5o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z5o, resolution 2.00Å" /> '''Crystal structure of...) |
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| - | [[Image:1z5o.gif|left|200px]]<br /><applet load="1z5o" size=" | + | [[Image:1z5o.gif|left|200px]]<br /><applet load="1z5o" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1z5o, resolution 2.00Å" /> | caption="1z5o, resolution 2.00Å" /> | ||
'''Crystal structure of MTA/AdoHcy nucleosidase Asp197Asn mutant complexed with 5'-methylthioadenosine'''<br /> | '''Crystal structure of MTA/AdoHcy nucleosidase Asp197Asn mutant complexed with 5'-methylthioadenosine'''<br /> | ||
==Overview== | ==Overview== | ||
| - | MTA/AdoHcy nucleosidase (MTAN) irreversibly hydrolyzes the N9-C1' bond in | + | 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== | ==About this Structure== | ||
| - | 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 MTA 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cornell, K | + | [[Category: Cornell, K A.]] |
[[Category: Horvatin, C.]] | [[Category: Horvatin, C.]] | ||
| - | [[Category: Howell, P | + | [[Category: Howell, P L.]] |
| - | [[Category: Huang, D | + | [[Category: Huang, D J.T.]] |
| - | [[Category: Lee, J | + | [[Category: Lee, J E.]] |
| - | [[Category: Riscoe, M | + | [[Category: Riscoe, M K.]] |
| - | [[Category: Smith, G | + | [[Category: Smith, G D.]] |
[[Category: MTA]] | [[Category: MTA]] | ||
[[Category: mixed alpha/beta]] | [[Category: mixed alpha/beta]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:15 2008'' |
Revision as of 14:12, 21 February 2008
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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 with as ligand. Active as Adenosylhomocysteine nucleosidase, with EC number 3.2.2.9 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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