1KMQ

Crystal Structure of a Constitutively Activated RhoA Mutant (Q63L)

Summary for 1KMQ

• Entry DOI: 10.2210/pdb1kmq/pdb
• Descriptor: TRANSFORMING PROTEIN RHOA, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, ... (5 entities in total)
• Functional Keywords: gtpase, constitutive mutant, gtp-analog, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Lipid-anchor; Cytoplasmic side: P61586
• Total number of polymer chains: 1
• Total formula weight: 21393.65

Authors

Longenecker, K.,Read, P.,Lin, S.-K.,Somlyo, A.P.,Nakamoto, R.K.,Derewenda, Z.S. (deposition date: 2001-12-17, release date: 2003-05-06, Last modification date: 2024-02-14)

Primary citation

Longenecker, K.,Read, P.,Lin, S.K.,Somlyo, A.P.,Nakamoto, R.K.,Derewenda, Z.S.
Structure of a constitutively activated RhoA mutant (Q63L) at 1.55 A resolution.
Acta Crystallogr.,Sect.D, 59:876-880, 2003

PubMed Abstract: Mutants of the small G protein RhoA that are deficient in GTPase activity and thereby exhibit constitutive molecular signaling activity are commonly used to discover its cellular functions. In particular, two such mutants, Gly14-->Val (G14V) and Gln63-->Leu (Q63L), are often used interchangeably for such studies. However, while their in vitro rates of GTP hydrolysis are very similar, differences are observed in their other functional properties. The structure of G14V-RhoA is known; in order to assess whether structural variations are responsible for functional differences, the crystal structure of a Q63L-RhoA bound to the GTP-analog 5'-guanylylimidodiphosphate (GMPPNP) was determined at 1.5 A resolution. Overall, the structure is very similar to that of G14V-RhoA, but the significantly higher resolution data permit an improved basis for structural analysis and comparison. The data support the notion that differences observed between the mutants in vivo are likely to arise from altered affinities for RhoGDI and not from direct structural differences.

PubMed: 12777804
DOI: 10.1107/S0907444903005390

Experimental method

X-RAY DIFFRACTION (1.55 Å)