2nt8: Difference between revisions

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==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.

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==

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[[Category: Lactobacillus reuteri]]

[[Category: Single protein]]

[[Category: Escalante-Semerena, J.C.]]

[[Category: Escalante-Semerena, J C.]]

[[Category: Mera, P.E.]]

[[Category: Mera, P E.]]

[[Category: Rayment, I.]]

[[Category: Sesma, F.]]

[[Category: St-Maurice, M.]]

[[Category: Taranto, M.P.]]

[[Category: Taranto, M P.]]

[[Category: ATP]]

[[Category: GOL]]

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[[Category: atp binding]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Lactobacillus reuteri]]
 [[Category: Single protein]]
-[[Category: Escalante-Semerena, J.C.]]
+[[Category: Escalante-Semerena, J C.]]
-[[Category: Mera, P.E.]]
+[[Category: Mera, P E.]]
 [[Category: Rayment, I.]]
 [[Category: Sesma, F.]]
 [[Category: St-Maurice, M.]]
-[[Category: Taranto, M.P.]]
+[[Category: Taranto, M P.]]
 [[Category: ATP]]
 [[Category: GOL]]
@@ Line 26: / Line 26: @@
 [[Category: atp binding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:24:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:10:45 2008''