1nmt

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[[Image:1nmt.png|left|200px]]
 
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{{STRUCTURE_1nmt| PDB=1nmt | SCENE= }}
{{STRUCTURE_1nmt| PDB=1nmt | SCENE= }}
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===N-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 A===
===N-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 A===
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{{ABSTRACT_PUBMED_9501915}}
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==Function==
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[[http://www.uniprot.org/uniprot/NMT_CANAL NMT_CANAL]] Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Substrate specificity requires an N-terminal glycine in the nascent polypeptide substrates. Ser is present at position 5 in almost all known N-myristoyl proteins and Lys is commonly encountered at postion 6. Basic residues are preferred at positions 7 and 8.<ref>PMID:1569105</ref> <ref>PMID:8300631</ref> <ref>PMID:9115247</ref>
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{{ABSTRACT_PUBMED_9501915}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:009501915</ref><ref group="xtra">PMID:011742118</ref><references group="xtra"/>
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<ref group="xtra">PMID:009501915</ref><references group="xtra"/><references/>
[[Category: Candida albicans]]
[[Category: Candida albicans]]
[[Category: Glycylpeptide N-tetradecanoyltransferase]]
[[Category: Glycylpeptide N-tetradecanoyltransferase]]

Revision as of 10:39, 16 April 2014

Template:STRUCTURE 1nmt

Contents

N-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 A

Template:ABSTRACT PUBMED 9501915

Function

[NMT_CANAL] Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Substrate specificity requires an N-terminal glycine in the nascent polypeptide substrates. Ser is present at position 5 in almost all known N-myristoyl proteins and Lys is commonly encountered at postion 6. Basic residues are preferred at positions 7 and 8.[1] [2] [3]

About this Structure

1nmt is a 3 chain structure with sequence from Candida albicans. Full crystallographic information is available from OCA.

Reference

  • Weston SA, Camble R, Colls J, Rosenbrock G, Taylor I, Egerton M, Tucker AD, Tunnicliffe A, Mistry A, Mancia F, de la Fortelle E, Irwin J, Bricogne G, Pauptit RA. Crystal structure of the anti-fungal target N-myristoyl transferase. Nat Struct Biol. 1998 Mar;5(3):213-21. PMID:9501915
  1. Wiegand RC, Carr C, Minnerly JC, Pauley AM, Carron CP, Langner CA, Duronio RJ, Gordon JI. The Candida albicans myristoyl-CoA:protein N-myristoyltransferase gene. Isolation and expression in Saccharomyces cerevisiae and Escherichia coli. J Biol Chem. 1992 Apr 25;267(12):8591-8. PMID:1569105
  2. Lodge JK, Johnson RL, Weinberg RA, Gordon JI. Comparison of myristoyl-CoA:protein N-myristoyltransferases from three pathogenic fungi: Cryptococcus neoformans, Histoplasma capsulatum, and Candida albicans. J Biol Chem. 1994 Jan 28;269(4):2996-3009. PMID:8300631
  3. McWherter CA, Rocque WJ, Zupec ME, Freeman SK, Brown DL, Devadas B, Getman DP, Sikorski JA, Gordon JI. Scanning alanine mutagenesis and de-peptidization of a Candida albicans myristoyl-CoA:protein N-myristoyltransferase octapeptide substrate reveals three elements critical for molecular recognition. J Biol Chem. 1997 May 2;272(18):11874-80. PMID:9115247

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