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.


3bfp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3bfp.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3bfp.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3bfp| PDB=3bfp | SCENE= }}
{{STRUCTURE_3bfp| PDB=3bfp | SCENE= }}
-
'''Crystal Structure of apo-PglD from Campylobacter jejuni'''
+
===Crystal Structure of apo-PglD from Campylobacter jejuni===
-
==Overview==
+
<!--
-
Campylobacter jejuni is highly unusual among bacteria in forming N-linked glycoproteins. The heptasaccharide produced by its pgl system is attached to protein Asn through its terminal 2,4-diacetamido-2,4,6-trideoxy-d-Glc (QuiNAc4NAc or N,N'-diacetylbacillosamine) moiety. The crucial, last part of this sugar's synthesis is the acetylation of UDP-2-acetamido-4-amino-2,4,6-trideoxy-d-Glc by the enzyme PglD, with acetyl-CoA as a cosubstrate. We have determined the crystal structures of PglD in CoA-bound and unbound forms, refined to 1.8 and 1.75 A resolution, respectively. PglD is a trimer of subunits each comprised of two domains, an N-terminal alpha/beta-domain and a C-terminal left-handed beta-helix. Few structural differences accompany CoA binding, except in the C-terminal region following the beta-helix (residues 189-195), which adopts an extended structure in the unbound form and folds to extend the beta-helix upon binding CoA. Computational molecular docking suggests a different mode of nucleotide-sugar binding with respect to the acetyl-CoA donor, with the molecules arranged in an "L-shape", compared with the "in-line" orientation in related enzymes. Modeling indicates that the oxyanion intermediate would be stabilized by the NH group of Gly143', with His125' the most likely residue to function as a general base, removing H+ from the amino group prior to nucleophilic attack at the carbonyl carbon of acetyl-CoA. Site-specific mutations of active site residues confirmed the importance of His125', Glu124', and Asn118. We conclude that Asn118 exerts its function by stabilizing the intricate hydrogen bonding network within the active site and that Glu124' may function to increase the pKa of the putative general base, His125'.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18198901}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18198901 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18198901}}
==About this Structure==
==About this Structure==
Line 39: Line 43:
[[Category: N-glycan biosynthesis]]
[[Category: N-glycan biosynthesis]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:43:18 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:37:44 2008''

Revision as of 06:37, 29 July 2008

Image:3bfp.png

Template:STRUCTURE 3bfp

Crystal Structure of apo-PglD from Campylobacter jejuni

Template:ABSTRACT PUBMED 18198901

About this Structure

3BFP is a Single protein structure of sequence from Campylobacter jejuni. Full crystallographic information is available from OCA.

Reference

Structure and Active Site Residues of PglD, an N-Acetyltransferase from the Bacillosamine Synthetic Pathway Required for N-Glycan Synthesis in Campylobacter jejuni(,)., Rangarajan ES, Ruane KM, Sulea T, Watson DC, Proteau A, Leclerc S, Cygler M, Matte A, Young NM, Biochemistry. 2008 Feb 19;47(7):1827-1836. Epub 2008 Jan 17. PMID:18198901

Page seeded by OCA on Tue Jul 29 09:37:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3bfp"
Personal tools