This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fan, J.
Right arrow Articles by Niu, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fan, J.
Right arrow Articles by Niu, L.

 Previous Article  |  Next Article 

Journal of Bacteriology, May 2007, p. 3573-3580, Vol. 189, No. 9
0021-9193/07/$08.00+0     doi:10.1128/JB.01083-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Crystal Structure of Uroporphyrinogen Decarboxylase from Bacillus subtilis{triangledown}

Jun Fan,1,2 Qun Liu,3 Quan Hao,3 Maikun Teng,1,2* and Liwen Niu1,2*

Hefei National Laboratory of Physical Sciences at Microscale and School of Life Sciences, University of Science & Technology of China, Hefei Anhui, 230027, China,1 Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, Anhui, 230037, China,2 MacCHESS, Cornell High Energy Synchrotron Source, Cornell University, Ithaca, New York 148533

Received 2 August 2006/ Accepted 12 November 2006

Uroporphyrinogen decarboxylase (UROD) is a branch point enzyme in the biosynthesis of the tetrapyrroles. It catalyzes the decarboxylation of four acetate groups of uroporphyrinogen III to yield coproporphyrinogen III, leading to heme and chlorophyll biosynthesis. UROD is a special type of nonoxidative decarboxylase, since no cofactor is essential for catalysis. In this work, the first crystal structure of a bacterial UROD, Bacillus subtilis UROD (URODBs), has been determined at a 2.3 Å resolution. The biological unit of URODBs was determined by dynamic light scattering measurements to be a homodimer in solution. There are four molecules in the crystallographic asymmetric unit, corresponding to two homodimers. Structural comparison of URODBs with eukaryotic URODs reveals a variation of two loops, which possibly affect the binding of substrates and release of products. Structural comparison with the human UROD-coproporphyrinogen III complex discloses a similar active cleft, with five invariant polar residues (Arg29, Arg33, Asp78, Tyr154, and His322) and three invariant hydrophobic residues (Ile79, Phe144, and Phe207), in URODBs. Among them, Asp78 may interact with the pyrrole NH groups of the substrate, and Arg29 is a candidate for positioning the acetate groups of the substrate. Both residues may also play catalytic roles.

* Corresponding author. Mailing address: Hefei National laboratory of Physical Sciences at Microscale and School of Life Sciences, University of Science & Technology of China, Hefei Anhui, 230027, China. Phone and fax for Maikun Teng: 86-551-3606314. E-mail: mkteng{at}ustc.edu.cn. Phone and fax for Liwen Niu: 86-551-3603046. E-mail: lwniu{at}ustc.edu.cn

{triangledown} Published ahead of print on 22 November 2006.

Journal of Bacteriology, May 2007, p. 3573-3580, Vol. 189, No. 9
0021-9193/07/$08.00+0     doi:10.1128/JB.01083-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»