1UH9
Crystal structure of rhizopuspepsin at pH 7.0
Summary for 1UH9
| Entry DOI | 10.2210/pdb1uh9/pdb |
| Related | 1UH7 1UH8 2APR |
| Descriptor | hizopuspepsin I (2 entities in total) |
| Functional Keywords | pepsin, aspartic proteinase, hydrolase |
| Biological source | Rhizopus microsporus var. chinensis |
| Total number of polymer chains | 1 |
| Total formula weight | 34312.92 |
| Authors | Prasad, B.V.L.S.,Suguna, K. (deposition date: 2003-06-26, release date: 2004-06-26, Last modification date: 2024-10-23) |
| Primary citation | Prasad, B.V.,Suguna, K. Effect of pH on the structure of rhizopuspepsin. Acta Crystallogr.,Sect.D, 59:1755-1761, 2003 Cited by PubMed Abstract: The crystal structure of rhizopuspepsin has been determined at three different pH values (4.6, 7.0 and 8.0) and compared with the previously reported structure at pH 6.0. A pH-sensitive region in the protein has been identified where certain structural changes take place at pH 8.0. An increase in the mobility of loops, weakening of hydrogen bonding and ionic interactions and a change in the water structure have been observed in this region. The loop between the first and the second beta-strands of the N-terminus shows increased mobility at high pH. This loop is known to be highly flexible in aspartic proteinases, aiding in relocating the N-terminal beta-strand segment in pH-related structural transformations. The observed changes in rhizopuspepsin indicate the triggering of a possible denatured state by high pH. The conformation of the active aspartates and the geometry of the catalytic site exhibit remarkable rigidity in this pH range. PubMed: 14501114DOI: 10.1107/S0907444903016068 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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