1y3h: Difference between revisions

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Crystal Structure of Inorganic Polyphosphate/ATP-NAD kinase from Mycobacterium tuberculosis

OverviewOverview

NAD kinase is a key enzyme in NADP biosynthesis. We solved the crystal structure of polyphosphate/ATP-NAD kinase from Mycobacterium tuberculosis (Ppnk) complexed with NAD (Ppnk-NAD) at 2.6A resolution using apo-Ppnk structure solved in this work, and revealed the details of the structure and NAD-binding site. Superimposition of tertiary structures of apo-Ppnk and Ppnk-NAD demonstrated a substantial conformational difference in a loop (Ppnk-flexible loop). As a quaternary structure, these Ppnk structures exhibited tetramer as in solution condition. Notably, the Ppnk-flexible loop was involved in the intersubunit contact and probably related to the NAD-binding of the other subunit. Furthermore, the two residues (Asp189, His226) substantially contributed to creating NAD-binding site on the other subunit. The two residues and the residues involved in NAD-binding were conserved. However, residues corresponding to the Ppnk-flexible loop were not conserved, making us to speculate that the Ppnk-flexible loop may be Ppnk-specific.

About this StructureAbout this Structure

1Y3H is a Single protein structure of sequence from Mycobacterium tuberculosis. Active as NAD(+) kinase, with EC number 2.7.1.23 Full crystallographic information is available from OCA.

ReferenceReference

NAD-binding mode and the significance of intersubunit contact revealed by the crystal structure of Mycobacterium tuberculosis NAD kinase-NAD complex., Mori S, Yamasaki M, Maruyama Y, Momma K, Kawai S, Hashimoto W, Mikami B, Murata K, Biochem Biophys Res Commun. 2005 Feb 11;327(2):500-8. PMID:15629142

Page seeded by OCA on Thu Feb 21 16:01:25 2008

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OCA

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-[[Image:1y3h.gif|left|200px]]<br /><applet load="1y3h" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1y3h.gif|left|200px]]<br /><applet load="1y3h" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1y3h, resolution 2.80&Aring;" />
 '''Crystal Structure of Inorganic Polyphosphate/ATP-NAD kinase from Mycobacterium tuberculosis'''<br />
 ==Overview==
-NAD kinase is a key enzyme in NADP biosynthesis. We solved the crystal, structure of polyphosphate/ATP-NAD kinase from Mycobacterium tuberculosis, (Ppnk) complexed with NAD (Ppnk-NAD) at 2.6A resolution using apo-Ppnk, structure solved in this work, and revealed the details of the structure, and NAD-binding site. Superimposition of tertiary structures of apo-Ppnk, and Ppnk-NAD demonstrated a substantial conformational difference in a, loop (Ppnk-flexible loop). As a quaternary structure, these Ppnk, structures exhibited tetramer as in solution condition. Notably, the, Ppnk-flexible loop was involved in the intersubunit contact and probably, related to the NAD-binding of the other subunit. Furthermore, the two, residues (Asp189, His226) substantially contributed to creating, NAD-binding site on the other subunit. The two residues and the residues, involved in NAD-binding were conserved. However, residues corresponding to, the Ppnk-flexible loop were not conserved, making us to speculate that the, Ppnk-flexible loop may be Ppnk-specific.
+NAD kinase is a key enzyme in NADP biosynthesis. We solved the crystal structure of polyphosphate/ATP-NAD kinase from Mycobacterium tuberculosis (Ppnk) complexed with NAD (Ppnk-NAD) at 2.6A resolution using apo-Ppnk structure solved in this work, and revealed the details of the structure and NAD-binding site. Superimposition of tertiary structures of apo-Ppnk and Ppnk-NAD demonstrated a substantial conformational difference in a loop (Ppnk-flexible loop). As a quaternary structure, these Ppnk structures exhibited tetramer as in solution condition. Notably, the Ppnk-flexible loop was involved in the intersubunit contact and probably related to the NAD-binding of the other subunit. Furthermore, the two residues (Asp189, His226) substantially contributed to creating NAD-binding site on the other subunit. The two residues and the residues involved in NAD-binding were conserved. However, residues corresponding to the Ppnk-flexible loop were not conserved, making us to speculate that the Ppnk-flexible loop may be Ppnk-specific.
 ==About this Structure==
-Y3H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Active as [http://en.wikipedia.org/wiki/NAD(+)_kinase NAD(+) kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.23 2.7.1.23] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y3H OCA].
+Y3H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Active as [http://en.wikipedia.org/wiki/NAD(+)_kinase NAD(+) kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.23 2.7.1.23] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y3H OCA].
 ==Reference==
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 [[Category: polyphosphate]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:32:35 2007''
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