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Crystal structure confirmation of JHP933 as a nucleotidyltransferase superfamily protein from Helicobacter pylori strain J99.

Zhao Y, Ye X, Su Y, Sun L, She F, Wu Y - PLoS ONE (2014)

Bottom Line: Studies suggested that certain genes in this region may play key roles in the pathogenesis of H. pylori-associated gastroduodenal diseases.A superposition demonstrates overall structural homology of the JHP933 N-terminal fragment with lincosamide antibiotic adenylyltransferase LinA and identifies a possible substrate-binding cleft of JHP933.Furthermore, through structural comparison with LinA and LinB, we pinpoint conservative active site residues which may contribute to divalent ion coordination and substrate binding.

View Article: PubMed Central - PubMed

Affiliation: State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou, Fujian, China.

ABSTRACT
Helicobacter pylori is a well-known pathogen involved in the development of peptic ulcer, gastric adenocarcinoma and other forms of gastric cancer. Recently, there has been more considerable interest in strain-specific genes located in plasticity regions with great genetic variability. However, little is known about many of these genes. Studies suggested that certain genes in this region may play key roles in the pathogenesis of H. pylori-associated gastroduodenal diseases. JHP933, a conserved putative protein of unknown function, is encoded by the gene in plasticity region of H. pylori strain J99. Here we have determined the structure of JHP933. Our work demonstrates that JHP933 is a nucleotidyltransferase superfamily protein with a characteristic αβαβαβα topology. A superposition demonstrates overall structural homology of the JHP933 N-terminal fragment with lincosamide antibiotic adenylyltransferase LinA and identifies a possible substrate-binding cleft of JHP933. Furthermore, through structural comparison with LinA and LinB, we pinpoint conservative active site residues which may contribute to divalent ion coordination and substrate binding.

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Overall structure of JHP933.Ribbon diagram of the JHP933 structure, N-terminal core domain is colored in lime and C-terminal tail domain in cyan. α-helices are labelled with α, β-strands are labelled with β, and 310 helices are labelled with η.
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pone-0104609-g001: Overall structure of JHP933.Ribbon diagram of the JHP933 structure, N-terminal core domain is colored in lime and C-terminal tail domain in cyan. α-helices are labelled with α, β-strands are labelled with β, and 310 helices are labelled with η.

Mentions: The overall structure of JHP933 consists of two domains: an N-terminal core domain and a C-terminal tail domain [Fig. 1]. The N-terminal core domain covers residues 11–170 and contains 5 α-helices (α1–α5) and 7 β-strands (β1–β7). A 310 helix (η1) connects β-strands β5 and β6. The C-terminal tail domain is formed by α-helices α6–α7 followed by an extended α-helix (α8). The two domains are connected by another 310 helix (η2) between α-helices α5 and α6.


Crystal structure confirmation of JHP933 as a nucleotidyltransferase superfamily protein from Helicobacter pylori strain J99.

Zhao Y, Ye X, Su Y, Sun L, She F, Wu Y - PLoS ONE (2014)

Overall structure of JHP933.Ribbon diagram of the JHP933 structure, N-terminal core domain is colored in lime and C-terminal tail domain in cyan. α-helices are labelled with α, β-strands are labelled with β, and 310 helices are labelled with η.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4125220&req=5

pone-0104609-g001: Overall structure of JHP933.Ribbon diagram of the JHP933 structure, N-terminal core domain is colored in lime and C-terminal tail domain in cyan. α-helices are labelled with α, β-strands are labelled with β, and 310 helices are labelled with η.
Mentions: The overall structure of JHP933 consists of two domains: an N-terminal core domain and a C-terminal tail domain [Fig. 1]. The N-terminal core domain covers residues 11–170 and contains 5 α-helices (α1–α5) and 7 β-strands (β1–β7). A 310 helix (η1) connects β-strands β5 and β6. The C-terminal tail domain is formed by α-helices α6–α7 followed by an extended α-helix (α8). The two domains are connected by another 310 helix (η2) between α-helices α5 and α6.

Bottom Line: Studies suggested that certain genes in this region may play key roles in the pathogenesis of H. pylori-associated gastroduodenal diseases.A superposition demonstrates overall structural homology of the JHP933 N-terminal fragment with lincosamide antibiotic adenylyltransferase LinA and identifies a possible substrate-binding cleft of JHP933.Furthermore, through structural comparison with LinA and LinB, we pinpoint conservative active site residues which may contribute to divalent ion coordination and substrate binding.

View Article: PubMed Central - PubMed

Affiliation: State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou, Fujian, China.

ABSTRACT
Helicobacter pylori is a well-known pathogen involved in the development of peptic ulcer, gastric adenocarcinoma and other forms of gastric cancer. Recently, there has been more considerable interest in strain-specific genes located in plasticity regions with great genetic variability. However, little is known about many of these genes. Studies suggested that certain genes in this region may play key roles in the pathogenesis of H. pylori-associated gastroduodenal diseases. JHP933, a conserved putative protein of unknown function, is encoded by the gene in plasticity region of H. pylori strain J99. Here we have determined the structure of JHP933. Our work demonstrates that JHP933 is a nucleotidyltransferase superfamily protein with a characteristic αβαβαβα topology. A superposition demonstrates overall structural homology of the JHP933 N-terminal fragment with lincosamide antibiotic adenylyltransferase LinA and identifies a possible substrate-binding cleft of JHP933. Furthermore, through structural comparison with LinA and LinB, we pinpoint conservative active site residues which may contribute to divalent ion coordination and substrate binding.

Show MeSH
Related in: MedlinePlus