1Y3H
Crystal Structure of Inorganic Polyphosphate/ATP-NAD kinase from Mycobacterium tuberculosis
Summary for 1Y3H
Entry DOI | 10.2210/pdb1y3h/pdb |
Related | 1Y3I |
Descriptor | Inorganic polyphosphate/ATP-NAD kinase (2 entities in total) |
Functional Keywords | nad kinase, polyphosphate, nad, atp, transferase |
Biological source | Mycobacterium tuberculosis |
Cellular location | Cytoplasm: P0A5S6 |
Total number of polymer chains | 2 |
Total formula weight | 65911.42 |
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 citation | Mori, 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: 15629142DOI: 10.1016/j.bbrc.2004.11.163 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
Download full validation report