6gx7

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Tubulin-CopN-alphaRep complex

Structural highlights

6gx7 is a 8 chain structure with sequence from Atcc vr-2282, Ovis aries and Synthetic construct sequences. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:GOL, GTP, MES, MG, PGE, SO4
Gene:lcrE, CP_0433, CPn_0324, BN1224_CV15_B_02610, BN1224_DC9_BL_00250, BN1224_GiD_A_03370, BN1224_H12_DC_00070, BN1224_MUL2216_E_00610, BN1224_Panola_E_01460, BN1224_PB1_B_03230, BN1224_U1271_C_01640, BN1224_UZG1_A_03360, BN1224_Wien2_E_01090, BN1224_YK41_BG_00220, CWL029c_C_01640 (ATCC VR-2282)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[D0VWZ0_SHEEP] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).[RuleBase:RU003505][SAAS:SAAS023123_004_019801] [D0VWY9_SHEEP] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity).[RuleBase:RU003505]

Publication Abstract from PubMed

Nucleation is one of the least understood steps of microtubule dynamics. It is a kinetically unfavorable process that is templated in the cell by the gamma-tubulin ring complex or by preexisting microtubules; it also occurs in vitro from pure tubulin. Here we study the nucleation inhibition potency of natural or artificial proteins in connection with their binding mode to the longitudinal surface of alpha- or beta-tubulin. The structure of tubulin-bound CopN, a Chlamydia protein that delays nucleation, suggests that this protein may interfere with two protofilaments at the (+) end of a nucleus. Designed ankyrin repeat proteins that share a binding mode similar to that of CopN also impede nucleation, whereas those that target only one protofilament do not. In addition, an alphaRep protein predicted to target two protofilaments at the (-) end does not delay nucleation, pointing to different behaviors at both ends of the nucleus. Our results link the interference with protofilaments at the (+) end and the inhibition of nucleation.

Insight into microtubule nucleation from tubulin-capping proteins.,Campanacci V, Urvoas A, Cantos-Fernandes S, Aumont-Nicaise M, Arteni AA, Velours C, Valerio-Lepiniec M, Dreier B, Pluckthun A, Pilon A, Pous C, Minard P, Gigant B Proc Natl Acad Sci U S A. 2019 Apr 29. pii: 1813559116. doi:, 10.1073/pnas.1813559116. PMID:31036638[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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References

  1. ↑ Campanacci V, Urvoas A, Cantos-Fernandes S, Aumont-Nicaise M, Arteni AA, Velours C, Valerio-Lepiniec M, Dreier B, Pluckthun A, Pilon A, Pous C, Minard P, Gigant B. Insight into microtubule nucleation from tubulin-capping proteins. Proc Natl Acad Sci U S A. 2019 Apr 29. pii: 1813559116. doi:, 10.1073/pnas.1813559116. PMID:31036638 doi:http://dx.doi.org/10.1073/pnas.1813559116

Contents


PDB ID 6gx7

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OCA

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