1QXP
Crystal Structure of a mu-like calpain
Summary for 1QXP
| Entry DOI | 10.2210/pdb1qxp/pdb |
| Related | 1DF0 1DKV |
| Descriptor | mu-like calpain (2 entities in total) |
| Functional Keywords | m-calpain, mu-calpain, catalytic triad, ca(2+) requirement, hydrolase chimera |
| Biological source | Rattus norvegicus (Norway rat) More |
| Total number of polymer chains | 2 |
| Total formula weight | 207019.92 |
| Authors | Pal, G.P.,Veyra, T.D.,Elce, J.S.,Jia, Z. (deposition date: 2003-09-08, release date: 2004-02-03, Last modification date: 2024-02-14) |
| Primary citation | Pal, G.P.,Veyra, T.D.,Elce, J.S.,Jia, Z. Crystal Structure of a mu-like calpain reveals a partially activated conformation with low Ca(2+) requirement Structure, 11:1521-1526, 2003 Cited by PubMed Abstract: The two Ca2+-dependent cysteine proteases, micro- and m-calpain, are involved in various Ca2+-linked signal pathways but differ markedly in their Ca2+ requirements for activation. We have determined the structure of a micro-like calpain, which has 85% micro-calpain sequence (the first 48 and the last 62 residues of the large subunit are those from m-calpain) and a low Ca2+ requirement. This construct was used because micro-calpain itself is too poorly expressed. The structure of micro-like calpain is very similar in overall fold to that of m-calpain as expected, but differs significantly in two aspects. In comparison with m-calpain, the catalytic triad residues in micro-like calpain, His and Cys, are much closer together in the absence of Ca2+, and significant portions of the Ca2+ binding EF-hand motifs are disordered and more flexible. These structural differences imply that Ca2+-free micro-calpain may represent a partially activated structure, requiring lower Ca2+ concentration to trigger its activation. PubMed: 14656436DOI: 10.1016/j.str.2003.11.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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