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1nmt

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Revision as of 07:04, 7 August 2019

N-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 A

Structural highlights

1nmt is a 3 chain structure with sequence from candida_stellatoidea Atcc 11006 candida stellatoidea . Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Glycylpeptide N-tetradecanoyltransferase, with EC number 2.3.1.97
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

N-myristoyl transferase (NMT) catalyzes the transfer of the fatty acid myristate from myristoyl-CoA to the N-terminal glycine of substrate proteins, and is found only in eukaryotic cells. The enzyme in this study is the 451 amino acid protein produced by Candida albicans, a yeast responsible for the majority of systemic infections in immuno-compromised humans. NMT activity is essential for vegetative growth, and the structure was determined in order to assist in the discovery of a selective inhibitor of NMT which could be developed as an anti-fungal drug. NMT has no sequence homology with other protein sequences and has a novel alpha/beta fold which shows internal two-fold symmetry, which may be a result of gene duplication. On one face of the protein there is a long, curved, relatively uncharged groove, at the center of which is a deep pocket. The pocket floor is negatively charged due to the vicinity of the C-terminal carboxylate and a nearby conserved glutamic acid residue, which separates the pocket from a cavity. These observations, considered alongside the positions of residues whose mutation affects substrate binding and activity, suggest that the groove and pocket are the sites of substrate binding and the floor of the pocket is the catalytic center.

Crystal structure of the anti-fungal target N-myristoyl transferase.,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 Nat Struct Biol. 1998 Mar;5(3):213-21. PMID:9501915^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ 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
↑ 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
↑ 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 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nmt"

@@ Line 1: / Line 1: @@
 ==N-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 A==
-<StructureSection load='1nmt' size='340' side='right' caption='[[1nmt]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
+<StructureSection load='1nmt' size='340' side='right'caption='[[1nmt]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1nmt]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11006_[[candida_stellatoidea]] Atcc 11006 [[candida stellatoidea]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NMT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NMT FirstGlance]. <br>
@@ Line 14: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nm/1nmt_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nm/1nmt_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 34: / Line 34: @@
 </StructureSection>
 [[Category: Glycylpeptide N-tetradecanoyltransferase]]
+[[Category: Large Structures]]
 [[Category: Pauptit, R A]]
 [[Category: Weston, S A]]

1nmt

From Proteopedia

Revision as of 07:04, 7 August 2019

N-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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