This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1iyk

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 09:58, 30 October 2019

Crystal structure of candida albicans N-myristoyltransferase with myristoyl-COA and peptidic inhibitor

Structural highlights

1iyk is a 2 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:	,
Related:	1iyl
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

Myristoyl-CoA:protein N-myristoyltransferase (Nmt) is a monomeric enzyme that catalyzes the transfer of the fatty acid myristate from myristoyl-CoA to the N-terminal glycine residue of a variety of eukaryotic and viral proteins. Genetic and biochemical studies have established that Nmt is an attractive target for antifungal drugs. We present here crystal structures of C. albicans Nmt complexed with two classes of inhibitor competitive for peptide substrates. One is a peptidic inhibitor designed from the peptide substrate; the other is a nonpeptidic inhibitor having a benzofuran core. Both inhibitors are bound into the same binding groove, generated by some structural rearrangements of the enzyme, with the peptidic inhibitor showing a substrate-like binding mode and the nonpeptidic inhibitor binding differently. Further, site-directed mutagenesis for C. albicans Nmt has been utilized in order to define explicitly which amino acids are critical for inhibitor binding. The results suggest that the enzyme has some degree of flexibility for substrate binding and provide valuable information for inhibitor design.

Crystal structures of Candida albicans N-myristoyltransferase with two distinct inhibitors.,Sogabe S, Masubuchi M, Sakata K, Fukami TA, Morikami K, Shiratori Y, Ebiike H, Kawasaki K, Aoki Y, Shimma N, D'Arcy A, Winkler FK, Banner DW, Ohtsuka T Chem Biol. 2002 Oct;9(10):1119-28. PMID:12401496^[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
↑ Sogabe S, Masubuchi M, Sakata K, Fukami TA, Morikami K, Shiratori Y, Ebiike H, Kawasaki K, Aoki Y, Shimma N, D'Arcy A, Winkler FK, Banner DW, Ohtsuka T. Crystal structures of Candida albicans N-myristoyltransferase with two distinct inhibitors. Chem Biol. 2002 Oct;9(10):1119-28. PMID:12401496

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/1iyk"

@@ Line 1: / Line 1: @@
 ==Crystal structure of candida albicans N-myristoyltransferase with myristoyl-COA and peptidic inhibitor==
-<StructureSection load='1iyk' size='340' side='right' caption='[[1iyk]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='1iyk' size='340' side='right'caption='[[1iyk]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1iyk]] is a 2 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=1IYK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IYK FirstGlance]. <br>
@@ Line 35: / Line 35: @@
 </StructureSection>
 [[Category: Glycylpeptide N-tetradecanoyltransferase]]
+[[Category: Large Structures]]
 [[Category: Aoki, Y]]
 [[Category: Arcy, A D]]

1iyk

From Proteopedia

Revision as of 09:58, 30 October 2019

Crystal structure of candida albicans N-myristoyltransferase with myristoyl-COA and peptidic inhibitor

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox