2nt8

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(New page: 200px<br /><applet load="2nt8" size="350" color="white" frame="true" align="right" spinBox="true" caption="2nt8, resolution 1.680&Aring;" /> '''ATP bound at the ac...)
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==Overview==
==Overview==
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The three-dimensional crystal structure of the PduO-type corrinoid, adenosyltransferase from Lactobacillus reuteri (LrPduO) has been solved to, 1.68-A resolution. The functional assignment of LrPduO as a corrinoid, adenosyltransferase was confirmed by in vivo and in vitro evidence. The, enzyme has an apparent Km(ATP) of 2.2 microM and Km(Cobalamin) of 0.13, microM and a kcat of 0.025 s(-1). Co-crystallization of the enzyme with, Mg-ATP resulted in well-defined electron density for an N-terminal loop, that had been disordered in other PduO-type enzyme structures. This newly, defined N-terminal loop makes up the lower portion of the enzyme active, site with the other half being contributed from an adjacent subunit. These, results provide the first detailed description of the enzyme active site, for a PduO-type adenosyltransferase and identify a unique ATP binding, motif at the protein N terminus. The molecular architecture at the active, site offers valuable new insight into the role of various residues, responsible for the human disease methylmalonic aciduria.
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The three-dimensional crystal structure of the PduO-type corrinoid adenosyltransferase from Lactobacillus reuteri (LrPduO) has been solved to 1.68-A resolution. The functional assignment of LrPduO as a corrinoid adenosyltransferase was confirmed by in vivo and in vitro evidence. The enzyme has an apparent Km(ATP) of 2.2 microM and Km(Cobalamin) of 0.13 microM and a kcat of 0.025 s(-1). Co-crystallization of the enzyme with Mg-ATP resulted in well-defined electron density for an N-terminal loop that had been disordered in other PduO-type enzyme structures. This newly defined N-terminal loop makes up the lower portion of the enzyme active site with the other half being contributed from an adjacent subunit. These results provide the first detailed description of the enzyme active site for a PduO-type adenosyltransferase and identify a unique ATP binding motif at the protein N terminus. The molecular architecture at the active site offers valuable new insight into the role of various residues responsible for the human disease methylmalonic aciduria.
==About this Structure==
==About this Structure==
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[[Category: Lactobacillus reuteri]]
[[Category: Lactobacillus reuteri]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Escalante-Semerena, J.C.]]
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[[Category: Escalante-Semerena, J C.]]
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[[Category: Mera, P.E.]]
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[[Category: Mera, P E.]]
[[Category: Rayment, I.]]
[[Category: Rayment, I.]]
[[Category: Sesma, F.]]
[[Category: Sesma, F.]]
[[Category: St-Maurice, M.]]
[[Category: St-Maurice, M.]]
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[[Category: Taranto, M.P.]]
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[[Category: Taranto, M P.]]
[[Category: ATP]]
[[Category: ATP]]
[[Category: GOL]]
[[Category: GOL]]
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[[Category: atp binding]]
[[Category: atp binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:24:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:10:45 2008''

Revision as of 16:10, 21 February 2008


2nt8, resolution 1.680Å

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ATP bound at the active site of a PduO type ATP:co(I)rrinoid adenosyltransferase from Lactobacillus reuteri

Overview

The three-dimensional crystal structure of the PduO-type corrinoid adenosyltransferase from Lactobacillus reuteri (LrPduO) has been solved to 1.68-A resolution. The functional assignment of LrPduO as a corrinoid adenosyltransferase was confirmed by in vivo and in vitro evidence. The enzyme has an apparent Km(ATP) of 2.2 microM and Km(Cobalamin) of 0.13 microM and a kcat of 0.025 s(-1). Co-crystallization of the enzyme with Mg-ATP resulted in well-defined electron density for an N-terminal loop that had been disordered in other PduO-type enzyme structures. This newly defined N-terminal loop makes up the lower portion of the enzyme active site with the other half being contributed from an adjacent subunit. These results provide the first detailed description of the enzyme active site for a PduO-type adenosyltransferase and identify a unique ATP binding motif at the protein N terminus. The molecular architecture at the active site offers valuable new insight into the role of various residues responsible for the human disease methylmalonic aciduria.

About this Structure

2NT8 is a Single protein structure of sequence from Lactobacillus reuteri with , , and as ligands. Active as Cob(I)yrinic acid a,c-diamide adenosyltransferase, with EC number 2.5.1.17 Full crystallographic information is available from OCA.

Reference

Structural characterization of the active site of the PduO-type ATP:Co(I)rrinoid adenosyltransferase from Lactobacillus reuteri., St Maurice M, Mera PE, Taranto MP, Sesma F, Escalante-Semerena JC, Rayment I, J Biol Chem. 2007 Jan 26;282(4):2596-605. Epub 2006 Nov 22. PMID:17121823

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