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Cloning, expression, purification, crystallization and preliminary X-ray crystallographic study of molybdopterin synthase from Thermus thermophilus HB8

Kanaujia, Shankar Prasad and Ranjani, Chellamuthu Vasuki and Jeyakanthan, Jeyaraman and Ohmori, Miwa and Agari, Kazuko and Kitamura, Yoshiaki and Baba, Seiki and Ebihara, Akio and Shinkai, Akeo and Kuramitsu, Seiki and Shiro, Yoshitsugu and Sekar, Kanagaraj and Yokoyama, Shigeyuki (2007) Cloning, expression, purification, crystallization and preliminary X-ray crystallographic study of molybdopterin synthase from Thermus thermophilus HB8. In: Acta Crystallographica Section F-Structural Biology and Crystallization Communications, 63 (4). pp. 324-326.

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Abstract

Thermus thermophilus is a Gram-negative aerobic thermophilic eubacterium which can grow at temperatures ranging from 323 to 355 K. In addition to their importance in thermostability or adaptation strategies for survival at high temperatures, the thermostable enzymes in thermophilic organisms contribute to a wide range of biotechnological applications. The molybdenum cofactor in all three kingdoms consists of a tricyclic pyranopterin termed molybdopterin that bears the cis-dithiolene group responsible for molybdenum ligation. The crystals of molybdopterin synthase from T. thermophilus HB8 belong to the primitive monoclinic space group $P2_1$, with unit-cell parameters a = 33.94, b = 103.32, c = 59.59 $A^o$, \beta = $101.3^o$. Preliminary studies and molecularreplacement calculations reveal the presence of three monomers in the asymmetric unit.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to International Union of Crystallography.
Keywords: Thermophilic eubacteria;molybdenum cofactor;MPT biosynthesis.
Department/Centre: Division of Information Sciences > BioInformatics Centre
Date Deposited: 29 Jul 2008
Last Modified: 19 Sep 2010 04:48
URI: http://eprints.iisc.ernet.in/id/eprint/15284

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