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InterPro: IPR015870 UDP-3-O-acyl N-acetylglucosamine deacetylase, N-terminal

Protein matches Help

UniProtKB

Matches:

1042 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR015870 UDP-acyl_N-AcGlcN_deAcase_N

Secondary

IPR004463

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.30.230.20	UDP-acyl_N-AcGlcN_deAcase_N	1042
Signatures in BioMart

InterPro Relationships Help

Parent

IPR020568 Ribosomal protein S5 domain 2-type fold

Found in

IPR004463 UDP-3-O-acyl N-acetylglucosamine deacetylase

GO Term annotation Help

Process

GO:0009245 lipid A biosynthetic process

Function

GO:0008759 UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity

InterPro annotation

Entry Details in BioMart

Abstract

UDP-3-O-N-acetylglucosamine deacetylases are zinc-dependent metalloamidases that catalyse the second and committed step in the biosynthesis of lipid A. Lipid A anchors lipopolysaccharide (the major constituent of the outer membrane) into the membrane in Gram negative bacteria. LpxC shows no homology to mammalian metalloamidases and is essential for cell viability, making it an important target for the development of novel antibacterial compounds [1]. The structure of UDP-3-O-N-acetylglucosamine deacetylase (LpxC) from Aquifex aeolicus has a two-layer alpha/beta structure similar to that of the second domain of ribosomal protein S5, only in LpxC there is a duplication giving two structural repeats of this fold, each repeat being elaborated with additional structures forming the active site. LpxC contains a zinc-binding motif, which resides at the base of an active site cleft and adjacent to a hydrophobic tunnel occupied by a fatty acid [2]. This tunnel accounts for the specificity of LpxC toward substrates and inhibitors bearing appropriately positioned 3-O-fatty acid substituents [3].

This entry represents the N-terminal domain.

Structural links Help

PDB - click here

SCOP: d.14.1.7

CATH: 3.30.230.20

Database links Help

Enzyme: EC:3.5.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR015870

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A0B6E8 30S ribosomal protein S9P

O67648 UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase

P0C2G7 UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase

P72988 UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase

Q9TLX3 UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR020568	Ribosomal protein S5 domain 2-type fold
IPR004463	UDP-3-O-acyl N-acetylglucosamine deacetylase
IPR011334	UDP-3-O-acyl N-acetylglucosamine deacetylase, C-terminal
IPR015870	UDP-3-O-acyl N-acetylglucosamine deacetylase, N-terminal
IPR020574	Ribosomal protein S9, conserved site
IPR000754	Ribosomal protein S9
IPR014721	Ribosomal protein S5 domain 2-type fold, subgroup
IPR019958	Ribosomal protein S9, archaeal
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Coggins BE, McClerren AL, Jiang L, Li X, Rudolph J, Hindsgaul O, Raetz CR, Zhou P. Refined solution structure of the LpxC-TU-514 complex and pKa analysis of an active site histidine: insights into the mechanism and inhibitor design. Biochemistry 44 1114-26 2005 [PubMed: 15667205] http://dx.doi.org/10.1021/bi047820z
2.	Whittington DA, Rusche KM, Shin H, Fierke CA, Christianson DW. Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis. Proc. Natl. Acad. Sci. U.S.A. 100 8146-50 2003 [PubMed: 12819349] http://dx.doi.org/10.1073/pnas.1432990100
3.	Shin H, Gennadios HA, Whittington DA, Christianson DW. Amphipathic benzoic acid derivatives: synthesis and binding in the hydrophobic tunnel of the zinc deacetylase LpxC. Bioorg. Med. Chem. 15 2617-23 2007 [PubMed: 17296300] http://dx.doi.org/10.1016/j.bmc.2007.01.044

Additional Reading Open in usermanual
	Buetow L, Dawson A, Hunter WN. The nucleotide-binding site of Aquifex aeolicus LpxC. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 2006 1082-6 [PubMed: 17077484] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=17077484&action=stream&blobtype=pdf
	Gennadios HA, Christianson DW. Binding of uridine 5'-diphosphate in the "basic patch" of the zinc deacetylase LpxC and implications for substrate binding. Biochemistry 45 2006 15216-23 [PubMed: 17176043] http://dx.doi.org/10.1021/bi0619021
	Barb AW, Jiang L, Raetz CR, Zhou P. Structure of the deacetylase LpxC bound to the antibiotic CHIR-090: Time-dependent inhibition and specificity in ligand binding. Proc. Natl. Acad. Sci. U.S.A. 104 2007 18433-8 [PubMed: 18025458] http://dx.doi.org/10.1073/pnas.0709412104
	Gennadios HA, Whittington DA, Li X, Fierke CA, Christianson DW. Mechanistic inferences from the binding of ligands to LpxC, a metal-dependent deacetylase. Biochemistry 45 2006 7940-8 [PubMed: 16800620] http://dx.doi.org/10.1021/bi060823m

InterPro 23.1