Summary for 5D7Z
| Entry DOI | 10.2210/pdb5d7z/pdb |
| Descriptor | Lactoylglutathione lyase, NICKEL (II) ION, FORMIC ACID, ... (6 entities in total) |
| Functional Keywords | lyase |
| Biological source | Zea mays (Maize) |
| Total number of polymer chains | 1 |
| Total formula weight | 34185.22 |
| Authors | Gonzalez, J.M. (deposition date: 2015-08-14, release date: 2015-09-09, Last modification date: 2024-03-06) |
| Primary citation | Turra, G.L.,Agostini, R.B.,Fauguel, C.M.,Presello, D.A.,Andreo, C.S.,Gonzalez, J.M.,Campos-Bermudez, V.A. Structure of the novel monomeric glyoxalase I from Zea mays. Acta Crystallogr.,Sect.D, 71:2009-2020, 2015 Cited by PubMed Abstract: The glyoxalase system is ubiquitous among all forms of life owing to its central role in relieving the cell from the accumulation of methylglyoxal, a toxic metabolic byproduct. In higher plants, this system is upregulated under diverse metabolic stress conditions, such as in the defence response to infection by pathogenic microorganisms. Despite their proven fundamental role in metabolic stresses, plant glyoxalases have been poorly studied. In this work, glyoxalase I from Zea mays has been characterized both biochemically and structurally, thus reporting the first atomic model of a glyoxalase I available from plants. The results indicate that this enzyme comprises a single polypeptide with two structurally similar domains, giving rise to two lateral concavities, one of which harbours a functional nickel(II)-binding active site. The putative function of the remaining cryptic active site remains to be determined. PubMed: 26457425DOI: 10.1107/S1399004715015205 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.73 Å) |
Structure validation
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