Crystal Structure ofParacoccus denitrificansElectron Transfer Flavoprotein:  Structural and Electrostatic Analysis of a Conserved Flavin Binding Domain†,‡

The X-ray crystal structure of the dimerized atrial natriuretic factor (ANF) receptor hormone-binding domain has provided a first structural view of this anti-hypertensive receptor. The structure reveals a surprising evolutionary link to the periplasmic-binding protein fold family. Furthermore, the presence of a chloride ion in the membrane distal domain and the presence of a second putative effector pocket suggests that the extracellular domain of this receptor is allosterically regulated. The scope of this article is to extensively review the data published on this receptor and to correlate it with the hormone-binding domain structure. In addition, a more detailed description is provided of the important features of this structure including the different binding sites for the ANF hormone, chloride ion, putative effector pocket, glycosylation sites, and dimer interface.Key words: crystal structure, periplasmic-binding protein fold, guanylyl cyclase, hormone receptor.

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Crystal structure of the receptor-binding domain of human B7-2: Insights into organization and signaling

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.252771499 ◽

2003 ◽

Vol 100 (5) ◽

pp. 2586-2591 ◽

Cited By ~ 62

Author(s):

X. Zhang ◽

J.-C. D. Schwartz ◽

S. C. Almo ◽

S. G. Nathenson

Keyword(s):

Crystal Structure ◽

Receptor Binding ◽

Binding Domain ◽

Receptor Binding Domain

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Crystal structure of the N-terminal domain of VqsR fromPseudomonas aeruginosaat 2.1 Å resolution

Acta Crystallographica Section F Structural Biology Communications ◽

10.1107/s2053230x17009025 ◽

2017 ◽

Vol 73 (7) ◽

pp. 431-436

Author(s):

Qing He ◽

Kang Wang ◽

Tiantian Su ◽

Feng Wang ◽

Lichuan Gu ◽

...

Keyword(s):

Crystal Structure ◽

Sequence Similarity ◽

Transcriptional Regulator ◽

Binding Domain ◽

Structural Comparison ◽

Homoserine Lactones ◽

Terminal Domain ◽

C Terminus ◽

Common Motif ◽

The Common

VqsR is a quorum-sensing (QS) transcriptional regulator which controls QS systems (las,rhlandpqs) by directly downregulating the expression ofqscRinPseudomonas aeruginosa. As a member of the LuxR family of proteins, VqsR shares the common motif of a helix–turn–helix (HTH)-type DNA-binding domain at the C-terminus, while the function of its N-terminal domain remains obscure. Here, the crystal structure of the N-terminal domain of VqsR (VqsR-N; residues 1–193) was determined at a resolution of 2.1 Å. The structure is folded into a regular α–β–α sandwich topology, which is similar to the ligand-binding domain (LBD) of the LuxR-type QS receptors. Although their sequence similarity is very low, structural comparison reveals that VqsR-N has a conserved enclosed cavity which could recognize acyl-homoserine lactones (AHLs) as in other LuxR-type AHL receptors. The structure suggests that VqsR could be a potential AHL receptor.

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An enzyme captured in two conformational states: crystal structure ofS-adenosyl-L-homocysteine hydrolase fromBradyrhizobium elkanii

Acta Crystallographica Section D Biological Crystallography ◽

10.1107/s1399004715018659 ◽

2015 ◽

Vol 71 (12) ◽

pp. 2422-2432 ◽

Cited By ~ 6

Author(s):

Tomasz Manszewski ◽

Kriti Singh ◽

Barbara Imiolczyk ◽

Mariusz Jaskolski

Keyword(s):

Crystal Structure ◽

Enzymatic Reaction ◽

Binding Domain ◽

Dimerization Domain ◽

Biologically Relevant ◽

Cofactor Binding ◽

Enzymatic Regulation ◽

Ligand Free ◽

Substrate Binding Domain ◽

Methyl Group Transfer

S-Adenosyl-L-homocysteine hydrolase (SAHase) is involved in the enzymatic regulation ofS-adenosyl-L-methionine (SAM)-dependent methylation reactions. After methyl-group transfer from SAM,S-adenosyl-L-homocysteine (SAH) is formed as a byproduct, which in turn is hydrolyzed to adenosine (Ado) and homocysteine (Hcy) by SAHase. The crystal structure of BeSAHase, an SAHase fromBradyrhizobium elkanii, which is a nitrogen-fixing bacterial symbiont of legume plants, was determined at 1.7 Å resolution, showing the domain organization (substrate-binding domain, NAD+cofactor-binding domain and dimerization domain) of the subunits. The protein crystallized in its biologically relevant tetrameric form, with three subunits in a closed conformation enforced by complex formation with the Ado product of the enzymatic reaction. The fourth subunit is ligand-free and has an open conformation. The BeSAHase structure therefore provides a unique snapshot of the domain movement of the enzyme induced by the binding of its natural ligands.

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