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Structure paper

TitleAn evolutionarily conserved salt bridge stabilizes the active site for GTP hydrolysis in Rho GTPases.
Journal, issue, pagesJ. Biol. Chem., Vol. 302, Page 111260-111260, Year 2026
Publish dateJan 13, 2026 (structure data deposition date)
AuthorsMarcus, K. / Schwabe, M. / Knihtila, R. / Mattos, C.
External linksJ. Biol. Chem. / PubMed:41654137
MethodsX-ray diffraction
Resolution1.947 - 3 Å
Structure data

PDB-10dc:
H-Ras GTPase R68A bound to GppNHp
Method: X-RAY DIFFRACTION / Resolution: 2.08 Å

PDB-9n4a:
Wild-type RhoA GTPase bound to GppNHp
Method: X-RAY DIFFRACTION / Resolution: 1.947 Å

PDB-9n4b:
RhoA GTPase R70A bound to GTPgammaS
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-9n4c:
RhoA GTPase E102A bound to GTPgammaS
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-GNP:
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / GppNHp, GMPPNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-DIO:
1,4-DIETHYLENE DIOXIDE

ChemComp-GSP:
5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE

ChemComp-SO4:
SULFATE ION

ChemComp-IOD:
IODIDE ION

ChemComp-CL:
Unknown entry

ChemComp-NA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsHYDROLASE / SIGNALING PROTEIN / small GTPase / Ras GTPase / GTP analog / Rho GTPase

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