[NMR paper] Solution NMR structure of GATase subunit and structural basis of interaction between GATase and ATPPase subunits in a two-subunit-type GMPS from Methanocaldococcus jannaschii.
Solution NMR structure of GATase subunit and structural basis of interaction between GATase and ATPPase subunits in a two-subunit-type GMPS from Methanocaldococcus jannaschii.
Related ArticlesSolution NMR structure of GATase subunit and structural basis of interaction between GATase and ATPPase subunits in a two-subunit-type GMPS from Methanocaldococcus jannaschii.
Biochemistry. 2013 May 31;
Authors: Ali R, Kumar S, Balaram H, Sarma SP
Abstract
The solution structure of the monomeric glutamine amidotransferase (GATase) subunit of the Methanocaldococcus janaschii (Mj) guanosine monophosphate synthase (GMPS) has been determined using high-resolution nuclear magnetic resonance methods. Gel filtration chromatography and 15N backbone relaxation studies have shown that Mj GATase subunit is present in solution as a 21 kDa (188 residues) monomer. The ensemble of twenty lowest energy structures showed an rmsd of 0.35±0.06 Å for backbone and 0.8±0.06 Å for all heavy atoms. Furthermore, 99.4 % backbone dihedral angles are present in allowed region of the Ramachandran map, indicating the stereochemical quality of the structure. The tertiary structure of the GATase is composed of a seven-stranded mixed ?-sheet that is fenced by five ?-helices. The Mj GATase is similar in structure to the Pyrococcus horikoshi (Ph) GATase subunit. NMR chemical shift perturbation and changes in line width were monitored to identify residues on GATase that were responsible for interaction with magnesium and the ATPPase subunit respectively. These interaction studies showed that a common surface exists for the metal-ion binding as well as for the protein-protein interaction. The dissociation constant for the GATase-Mg2+ interaction has been found to be ~1mM, which implies that interaction is very weak and falls in fast chemical exchange regime. The GATase-ATPPase interaction on the other hand falls in intermediate chemical exchange regime on NMR time scale. The implication of this interaction on the regulation of the GATase activity of holo GMPS is discussed.
PMID: 23724776 [PubMed - as supplied by publisher]
Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.
Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.
Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.
J Struct Funct Genomics. 2011 Jul 23;
Authors: Eletsky A, Ruyechan WT, Xiao R, Acton TB, Montelione GT, Szyperski T
The solution NMR structure of protein MED25(391-543), comprising the activator interacting domain (ACID) of subunit 25 of the human mediator, is presented along with the measurement of...
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NMR solution structure of subunit E (fragment E(1-69)) of the Saccharomyces cerevisiae V (1)V (O) ATPase.
NMR solution structure of subunit E (fragment E(1-69)) of the Saccharomyces cerevisiae V (1)V (O) ATPase.
NMR solution structure of subunit E (fragment E(1-69)) of the Saccharomyces cerevisiae V (1)V (O) ATPase.
J Bioenerg Biomembr. 2011 Mar 12;
Authors: Rishikesan S, Thaker YR, Grüber G
The N-terminus of V-ATPase subunit E has been shown to associate with the subunits C, G and H, respectively. To understand the assembly of E with its neighboring subunits as well as its N-terminal structure, the N-terminal region, E(1-69), of the...
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[NMR paper] Structural characterization of the interaction of the delta and alpha subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy.
Structural characterization of the interaction of the delta and alpha subunits of the Escherichia coli F1F0-ATP synthase by NMR spectroscopy.
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Biochemistry. 2005 Sep 6;44(35):11786-94
Authors: Wilkens S, Borchardt D, Weber J, Senior AE
A critical point of interaction between F(1) and F(0) in the bacterial F(1)F(0)-ATP synthase is formed by the alpha and delta subunits. Previous work has...
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[NMR paper] Solution NMR structure and backbone dynamics of the PsaE subunit of photosystem I fro
Solution NMR structure and backbone dynamics of the PsaE subunit of photosystem I from Synechocystis sp. PCC 6803.
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Biochemistry. 2002 Nov 26;41(47):13902-14
Authors: Barth P, Savarin P, Gilquin B, Lagoutte B, Ochsenbein F
PsaE is a small peripheral subunit of photosystem I (PSI) that is very accessible to the surrounding medium. It plays an essential role in optimizing the interactions with the soluble electron...
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[NMR paper] NMR solution structure of the theta subunit of DNA polymerase III from Escherichia co
NMR solution structure of the theta subunit of DNA polymerase III from Escherichia coli.
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Protein Sci. 2000 Apr;9(4):721-33
Authors: Keniry MA, Berthon HA, Yang JY, Miles CS, Dixon NE
The catalytic core of Escherichia coli DNA polymerase III contains three tightly associated subunits (alpha, epsilon, and theta). The theta subunit is the smallest, but the least understood of the three. As a first step in a program aimed at understanding its...
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Solution structure of subunit F (Vma7p) of the eukaryotic V(1)V(O) ATPase from Saccha
Solution structure of subunit F (Vma7p) of the eukaryotic V(1)V(O) ATPase from Saccharomyces cerevesiae derived from SAXS and NMR spectroscopy.
Solution structure of subunit F (Vma7p) of the eukaryotic V(1)V(O) ATPase from Saccharomyces cerevesiae derived from SAXS and NMR spectroscopy.
Biochim Biophys Acta. 2010 Sep 11;
Authors: Basak S, Gayen S, Thaker YR, Manimekalai MS, Roessle M, Hunke C, Grüber G
Vacuolar ATPases uses the energy derived from ATP hydrolysis, catalyzed in the A(3)B(3) sector of the V(1) ATPase to pump protons via the...
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[NMR paper] Subunit association and structural analysis of platelet basic protein and related pro
Subunit association and structural analysis of platelet basic protein and related proteins investigated by 1H NMR spectroscopy and circular dichroism.
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J Biol Chem. 1994 Aug 5;269(31):20110-8
Authors: Yang Y, Mayo KH, Daly TJ, Barry JK, La Rosa GJ
Platelet basic protein (PBP) (94 residues) is naturally processed via N-terminal cleavage to yield connective tissue activating...
Solution NMR structure of GATase subunit and structural basis of interaction between GATase and ATPPase subunits in a two-subunit-type GMPS from Methanocaldococcus jannaschii.
Linear Mode
