2nmt: Difference between revisions

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New page: left|200px<br /><applet load="2nmt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nmt, resolution 2.90Å" /> '''MYRISTOYL-COA:PROTEI...
 
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[[Image:2nmt.jpg|left|200px]]<br /><applet load="2nmt" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2nmt.jpg|left|200px]]<br /><applet load="2nmt" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2nmt, resolution 2.90&Aring;" />
caption="2nmt, resolution 2.90&Aring;" />
'''MYRISTOYL-COA:PROTEIN N-MYRISTOYLTRANSFERASE BOUND TO MYRISTOYL-COA AND PEPTIDE ANALOGS'''<br />
'''MYRISTOYL-COA:PROTEIN N-MYRISTOYLTRANSFERASE BOUND TO MYRISTOYL-COA AND PEPTIDE ANALOGS'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
2NMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with NHM, MIM and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glycylpeptide_N-tetradecanoyltransferase Glycylpeptide N-tetradecanoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.97 2.3.1.97] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NMT OCA].  
2NMT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=NHM:'>NHM</scene>, <scene name='pdbligand=MIM:'>MIM</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glycylpeptide_N-tetradecanoyltransferase Glycylpeptide N-tetradecanoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.97 2.3.1.97] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NMT OCA].  


==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bhatnagar, R.S.]]
[[Category: Bhatnagar, R S.]]
[[Category: Fuetterer, K.]]
[[Category: Fuetterer, K.]]
[[Category: Waksman, G.]]
[[Category: Waksman, G.]]
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[[Category: transferase acyltransferase]]
[[Category: transferase acyltransferase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:48:08 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:08:36 2008''

Revision as of 19:08, 21 February 2008

File:2nmt.jpg


2nmt, resolution 2.90Å

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

OverviewOverview

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.

About this StructureAbout this Structure

2NMT is a Single protein structure of sequence from Saccharomyces cerevisiae with , and as ligands. Active as Glycylpeptide N-tetradecanoyltransferase, with EC number 2.3.1.97 Full crystallographic information is available from OCA.

ReferenceReference

Structure of N-myristoyltransferase with bound myristoylCoA and peptide substrate analogs., Bhatnagar RS, Futterer K, Farazi TA, Korolev S, Murray CL, Jackson-Machelski E, Gokel GW, Gordon JI, Waksman G, Nat Struct Biol. 1998 Dec;5(12):1091-7. PMID:9846880

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