Evidence map›Paper›PMID 18006497›Full record

ArticleThe Journal of biological chemistry2008

PAS-mediated dimerization of soluble guanylyl cyclase revealed by signal transduction histidine kinase domain crystal structure.

Xiaolei Ma, Nazish Sayed, Padmamalini Baskaran, Annie Beuve, Focco van den Akker

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
3.4field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

53 citing papers in PubMed, 92 citations in OpenAlex.

  1. Dimerization Rules of Mammalian PAS Proteins.Journal of molecular biology · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Xiaolei MaDepartment of Biochemistry/RT500, Case Western Reserve University, Cleveland, Ohio 44106, USA.
Nazish Sayed
Padmamalini Baskaran
Annie Beuve
Focco van den Akker
Case Western Reserve University · USRutgers New Jersey Medical SchoolRutgers, The State University of New Jersey · US

Funding

Regulation of Soluble Guanylyl Cyclase, the NO-ReceptorR01GM067640 · NIGMS · UNIV OF MED/DENT OF NJ-NJ MEDICAL SCHOOL · PI BEUVE, ANNIE V · 2003 to 2021
$5.8M
Soluble guanylyl cyclase: mechanisms of activation and modulationR01HL075329 · NHLBI · CASE WESTERN RESERVE UNIVERSITY · PI VAN DEN AKKER, FOCCO · 2005 to 2014
$2.7M
NHLBI NIH HHS R01 HL075329NIGMS NIH HHS R01 GM067640
6 · The paper itself

Abstract

Signal transduction histidine kinases (STHK) are key for sensing environmental stresses, crucial for cell survival, and attain their sensing ability using small molecule binding domains. The N-terminal domain in an STHK from Nostoc punctiforme is of unknown function yet is homologous to the central region in soluble guanylyl cyclase (sGC), the main receptor for nitric oxide (NO). This domain is termed H-NOXA (or H-NOBA) because it is often associated with the heme-nitric oxide/oxygen binding (H-NOX) domain. A structure-function approach was taken to investigate the role of H-NOXA in STHK and sGC. We report the 2.1 A resolution crystal structure of the dimerized H-NOXA domain of STHK, which reveals a Per-Arnt-Sim (PAS) fold. The H-NOXA monomers dimerize in a parallel arrangement juxtaposing their N-terminal helices and preceding residues. Such PAS dimerization is similar to that previously observed for EcDOS, AvNifL, and RmFixL. Deletion of 7 N-terminal residues affected dimer organization. Alanine scanning mutagenesis in sGC indicates that the H-NOXA domains of sGC could adopt a similar dimer organization. Although most putative interface mutations did decrease sGCbeta1 H-NOXA homodimerization, heterodimerization of full-length heterodimeric sGC was mostly unaffected, likely due to the additional dimerization contacts of sGC in the coiled-coil and catalytic domains. Exceptions are mutations sGCalpha1 F285A and sGCbeta1 F217A, which each caused a drastic drop in NO stimulated activity, and mutations sGCalpha1 Q368A and sGCbeta1 Q309A, which resulted in both a complete lack of activity and heterodimerization. Our structural and mutational results provide new insights into sGC and STHK dimerization and overall architecture.

Indexed as

Amino Acid SequenceAnimalsChlorocebus aethiopsConserved SequenceCOS CellsCrystallography, X-RayDimerizationGenomeGuanylate CyclaseHaplorhiniHistidine KinaseMolecular Sequence DataMutagenesisPeptide FragmentsProtein KinasesRatsGuanylate CyclaseHistidine KinasePeptide FragmentsProtein KinasesRecombinant Proteins

Identifiers

PMID18006497
PMCPMC3010369
OpenAlexW2061800171

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.