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      Why Hypothetical Protein KPN00728 of Klebsiella pneumoniae Should Be Classified as Chain C of Succinate Dehydrogenase?

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          Abstract

          Twenty percent of genes that encode for hypothetical proteins from Klebsiella pneumoniae MGH78578 were identified, leading to KPN00728 and KPN00729 after bioinformatics analysis. Both open reading frames showed high sequence homology to Succinate dehydrogenase Chain C (SdhC) and D (SdhD) from Escherichia coli. Recently, KPN00729 was assigned as SdhD. KPN00728 thus remains of particular interest as no annotated genes from the complete genome sequence encode for SdhC. We discovered KPN00728 has a missing region with conserved residues important for ubiquinone (UQ) and heme group binding. Structure and function prediction of KPN00728 coupled with secondary structure analysis and transmembrane topology showed KPN00728 adopts SDH-(subunit C)-like structure. To further probe its functionality, UQ was docked on the built model (consisting KPN00728 and KPN00729) and formation of hydrogen bonds between UQ and Ser27, Arg31 (KPN00728) and Tyr84 (KPN00729) further reinforces and supports that KPN00728 is indeed SDH. This is the first report on the structural and function prediction of KPN00728 of K. pneumoniae MGH78578 as SdhC.

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          Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function

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            Is Open Access

            The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data

            The worldwide Protein Data Bank (wwPDB) is the international collaboration that manages the deposition, processing and distribution of the PDB archive. The online PDB archive is a repository for the coordinates and related information for more than 38 000 structures, including proteins, nucleic acids and large macromolecular complexes that have been determined using X-ray crystallography, NMR and electron microscopy techniques. The founding members of the wwPDB are RCSB PDB (USA), MSD-EBI (Europe) and PDBj (Japan) [H.M. Berman, K. Henrick and H. Nakamura (2003) Nature Struct. Biol., 10, 980]. The BMRB group (USA) joined the wwPDB in 2006. The mission of the wwPDB is to maintain a single archive of macromolecular structural data that are freely and publicly available to the global community. Additionally, the wwPDB provides a variety of services to a broad community of users. The wwPDB website at provides information about services provided by the individual member organizations and about projects undertaken by the wwPDB.
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              AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules

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                Author and article information

                Contributors
                +60-4-6534533 , +60-4-6532206 , +60-4-6534531 , habibah@ipharm.gov.my , habibahw@usm.my
                Journal
                Protein J
                The Protein Journal
                Springer US (Boston )
                1572-3887
                1875-8355
                27 October 2009
                December 2009
                : 28
                : 9-10
                : 415-427
                Affiliations
                [1 ]Pharmaceutical Design and Simulation (PhDS) Laboratory, School of Pharmaceutical Sciences, Universiti Sains Malaysia, 11800 Minden, Pulau Pinang Malaysia
                [2 ]School of Biological Sciences, Universiti Sains Malaysia, 11800 Minden, Pulau Pinang Malaysia
                [3 ]Centre for Advanced Drug Delivery, Malaysian Institute of Pharmaceuticals and Nutraceuticals, Ministry of Science, Technology and Innovation, SAINS@USM, No 10, 11900 Persiaran Bukit Jambul, Pulau Pinang Malaysia
                Article
                9209
                10.1007/s10930-009-9209-9
                2785890
                19859792
                d198b229-0a48-4824-bfa2-b0d8112d2705
                © The Author(s) 2009
                History
                Categories
                Article
                Custom metadata
                © Springer Science+Business Media, LLC 2009

                Biochemistry
                molecular docking,sequence analysis,hypothetical protein,succinate dehydrogenase,structure prediction

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