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.

2p56

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 09:18, 18 October 2017

Crystal structure of alpha-2,3-sialyltransferase from Campylobacter jejuni in apo form

Structural highlights

2p56 is a 1 chain structure with sequence from "campylobacter_fetus_subsp._jejuni"_smibert_1974 "campylobacter fetus subsp. jejuni" smibert 1974. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	2p2v
Gene:	cst-I ("Campylobacter fetus subsp. jejuni" Smibert 1974)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Sialic acid is an essential sugar in biology that plays key roles in numerous cellular processes and interactions. The biosynthesis of sialylated glycoconjugates is catalyzed by five distinct families of sialyltransferases. In the last 25 years, there has been much research on the enzymes themselves, their genes, and their reaction products, but we still do not know the precise molecular mechanism of action for this class of glycosyltransferase. We previously reported the first detailed structural and kinetic characterization of Cst-II, a bifunctional sialyltransferase (CAZy GT-42) from the bacterium Campylobacter jejuni [Chiu et al. (2004) Nat. Struct. Mol. Biol. 11, 163-170]. This enzyme can use both Gal-beta-1,3/4-R and Neu5Ac-alpha-2,3-Gal-beta-1,3/4-R as acceptor sugars. A second sialyltransferase from this bacterium, Cst-I, has been shown to utilize solely Gal-beta-1,3/4-R as the acceptor sugar in its transferase reaction. We report here the structural and kinetic characterization of this monofunctional enzyme, which belongs to the same sialyltransferase family as Cst-II, in both apo and substrate bound form. Our structural data show that Cst-I adopts a similar GTA-type glycosyltransferase fold to that of the bifunctional Cst-II, with conservation of several key noncharged catalytic residues. Significant differences are found, however, between the two enzymes in the lid domain region, which is critical to the creation of the acceptor sugar binding site. Furthermore, molecular modeling of various acceptor sugars within the active sites of these enzymes provides significant new insights into the structural basis for substrate specificities within this biologically important enzyme class.

Structural analysis of the alpha-2,3-sialyltransferase Cst-I from Campylobacter jejuni in apo and substrate-analogue bound forms.,Chiu CP, Lairson LL, Gilbert M, Wakarchuk WW, Withers SG, Strynadka NC Biochemistry. 2007 Jun 19;46(24):7196-204. Epub 2007 May 23. PMID:17518445^[1]

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

References

↑ Chiu CP, Lairson LL, Gilbert M, Wakarchuk WW, Withers SG, Strynadka NC. Structural analysis of the alpha-2,3-sialyltransferase Cst-I from Campylobacter jejuni in apo and substrate-analogue bound forms. Biochemistry. 2007 Jun 19;46(24):7196-204. Epub 2007 May 23. PMID:17518445 doi:10.1021/bi602543d

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2p56"

@@ Line 1: / Line 1: @@
 ==Crystal structure of alpha-2,3-sialyltransferase from Campylobacter jejuni in apo form==
 <StructureSection load='2p56' size='340' side='right' caption='[[2p56]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2p2v|2p2v]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cst-I ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=197 "Campylobacter fetus subsp. jejuni" Smibert 1974])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p56 OCA], [http://pdbe.org/2p56 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p56 RCSB], [http://www.ebi.ac.uk/pdbsum/2p56 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2p56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p56 OCA], [http://pdbe.org/2p56 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p56 RCSB], [http://www.ebi.ac.uk/pdbsum/2p56 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2p56 ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==

2p56

From Proteopedia

Revision as of 09:18, 18 October 2017

Crystal structure of alpha-2,3-sialyltransferase from Campylobacter jejuni in apo form

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox