1nmt: Difference between revisions

Revision as of 05:47, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1nmt.png

Template:STRUCTURE 1nmt

N-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 AN-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 A

Template:ABSTRACT PUBMED 9501915

About this StructureAbout this Structure

1NMT is a Single protein structure of sequence from Candida albicans. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 29 05:47:03 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1nmt.jpg|left|200px]]
+{{Seed}}
+[[Image:1nmt.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1nmt|  PDB=1nmt  |  SCENE=  }}
-'''N-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 A'''
+===N-MYRISTOYL TRANSFERASE FROM CANDIDA ALBICANS AT 2.45 A===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9501915}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9501915 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9501915}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Myristylation]]
 [[Category: Transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:43:25 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:47:03 2008''