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1Y3H

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

Summary for 1Y3H
Entry DOI10.2210/pdb1y3h/pdb
Related1Y3I
DescriptorInorganic polyphosphate/ATP-NAD kinase (2 entities in total)
Functional Keywordsnad kinase, polyphosphate, nad, atp, transferase
Biological sourceMycobacterium tuberculosis
Cellular locationCytoplasm: P0A5S6
Total number of polymer chains2
Total formula weight65911.42
Authors
Mori, S.,Yamasaki, M.,Maruyama, Y.,Momma, K.,kawai, S.,Hashimoto, W.,Mikami, B.,Murata, K. (deposition date: 2004-11-24, release date: 2005-01-18, Last modification date: 2024-05-29)
Primary citationMori, S.,Yamasaki, M.,Maruyama, Y.,Momma, K.,Kawai, S.,Hashimoto, W.,Mikami, B.,Murata, K.
NAD-binding mode and the significance of intersubunit contact revealed by the crystal structure of Mycobacterium tuberculosis NAD kinase-NAD complex
BIOCHEM.BIOPHYS.RES.COMMUN., 327:500-508, 2005
Cited by
PubMed Abstract: 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.
PubMed: 15629142
DOI: 10.1016/j.bbrc.2004.11.163
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

226707

數據於2024-10-30公開中

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