2nmt: Difference between revisions

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[[Image:2nmt.jpg|left|200px]]
{{Seed}}
[[Image:2nmt.png|left|200px]]


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{{STRUCTURE_2nmt|  PDB=2nmt  |  SCENE=  }}  
{{STRUCTURE_2nmt|  PDB=2nmt  |  SCENE=  }}  


'''MYRISTOYL-COA:PROTEIN N-MYRISTOYLTRANSFERASE BOUND TO MYRISTOYL-COA AND PEPTIDE ANALOGS'''
===MYRISTOYL-COA:PROTEIN N-MYRISTOYLTRANSFERASE BOUND TO MYRISTOYL-COA AND PEPTIDE ANALOGS===




==Overview==
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N-myristoyltransferase (Nmt) attaches myristate to the N-terminal glycine of many important eukaryotic and viral proteins. It is a target for anti-fungal and anti-viral therapy. We have determined the structure, to 2.9 A resolution, of a ternary complex of Saccharomyces cerevisiae Nmt1p with bound myristoylCoA and peptide substrate analogs. The model reveals structural features that define the enzyme's substrate specificities and regulate the ordered binding and release of substrates and products. A novel catalytic mechanism is proposed involving deprotonation of the N-terminal ammonium of a peptide substrate by the enzyme's C-terminal backbone carboxylate.
The line below this paragraph, {{ABSTRACT_PUBMED_9846880}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9846880 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9846880}}


==About this Structure==
==About this Structure==
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[[Category: Waksman, G.]]
[[Category: Waksman, G.]]
[[Category: Transferase acyltransferase]]
[[Category: Transferase acyltransferase]]
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