A MOLECULAR MODELING STUDY ON BACTERIAL ACETATE KINASES: CHARACTERIZATION OF ACTIVE SITE WITH THE AIM OF INHIBITOR DESIGN

Q: How can I download an article?

To download an article from SID, first log in to the site, search for the article title, and click on the 'Download Article' option.

Q: How can I download an ISI article?

To download an ISI article on SID, enter the keyword or article title in the search bar, view the relevant results, click on the desired article, and select the 'Download Article' option.

Q: How can I access the SID database?

To access the SID database, visit SID.ir, create an account, and log in to access scientific resources.

Q: Is downloading articles from SID free?

Some articles on SID are available for free, while others require payment. Details are specified on the article's page.

ASGARI S.; EBRAHIM HABIBI A.; SHARIATI P.

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Journal Paper

Paper Information

Journal: IRANIAN JOURNAL OF BIOLOGY Year:2011 | Volume:24 | Issue:2 Page(s): 218-238

Download Full-Text

Persian Verion

View:

1,213

Download:

Cites:

Information Journal Paper

Title

A MOLECULAR MODELING STUDY ON BACTERIAL ACETATE KINASES: CHARACTERIZATION OF ACTIVE SITE WITH THE AIM OF INHIBITOR DESIGN

Author(s)

ASGARI S. | EBRAHIM HABIBI A. | SHARIATI P. | Issue Writer Certificate

Keywords

ACETATE KINASEQ2

MOLECULAR MODELINGQ2

Abstract

ACETATE KINASE, an enzyme widely distributed in the bacterial and archaeal domains, catalyzes the phosphorylation of acetate. Acetyl phosphate is a precursor of acetyl coenzyme A and a potential regulator of bacterial signal-transduction. To gain some insight into the structure-function relationship of this enzyme, A variety of Gram-positive and Gram-negative bacterial ACETATE KINASEs, as well as a fungal and an algal sequences were chosen and three-dimensional structures were generated for each sequence. Only one structure (Methanosarcina thermophila) has been elucidated so far by X-ray crystallography, which was used as a template. These 22 sequences presented between 53 and 76% similarity with that of the template enzyme. An average of 50 models were generated and refined for each sequence with the use of MOD ELLER 9v2, and checked with Procheck and Errat programs. The best models were then compared using the Chimera software. The obtained structures presented a fold similar to that of the template enzyme, with an average RMSD (Root Mean Square Deviation) of 0.46 AO only small differences could be detected mainly in the N-terminal part, far away from the active site. These occur in the connecting segments of beta-sheets 3 and 4 or 4 and 5, or in the loop positioned after helix 1. The acetate binding pocket is completely identical between all models, with the exception of some proteins possessing a His residue instead of ASh (126 in Methanosarcina).This structural comparison of various ACETATE KINASEs showing a highly conserved fold ,could be of use in the design of this enzyme inhibitors, acting on a broad range of microorganisms.

Cites

No record.

References

No record.

Cite

APA: Copy

ASGARI, S., EBRAHIM HABIBI, A., & SHARIATI, P.. (2011). A MOLECULAR MODELING STUDY ON BACTERIAL ACETATE KINASES: CHARACTERIZATION OF ACTIVE SITE WITH THE AIM OF INHIBITOR DESIGN. IRANIAN JOURNAL OF BIOLOGY, 24(2), 218-238. SID. https://sid.ir/paper/21199/en

Vancouver: Copy

ASGARI S., EBRAHIM HABIBI A., SHARIATI P.. A MOLECULAR MODELING STUDY ON BACTERIAL ACETATE KINASES: CHARACTERIZATION OF ACTIVE SITE WITH THE AIM OF INHIBITOR DESIGN. IRANIAN JOURNAL OF BIOLOGY[Internet]. 2011;24(2):218-238. Available from: https://sid.ir/paper/21199/en

IEEE: Copy

S. ASGARI, A. EBRAHIM HABIBI, and P. SHARIATI, “A MOLECULAR MODELING STUDY ON BACTERIAL ACETATE KINASES: CHARACTERIZATION OF ACTIVE SITE WITH THE AIM OF INHIBITOR DESIGN,” IRANIAN JOURNAL OF BIOLOGY, vol. 24, no. 2, pp. 218–238, 2011, [Online]. Available: https://sid.ir/paper/21199/en

Related Journal Papers