2W4D

Acylphosphatase variant G91A from Pyrococcus horikoshii

Summary for 2W4D

Entry DOI	10.2210/pdb2w4d/pdb
Related	1V3Z 1W2I 2W4C
Descriptor	ACYLPHOSPHATASE, POTASSIUM ION, PHOSPHATE ION, ... (4 entities in total)
Functional Keywords	hydrolase
Biological source	PYROCOCCUS HORIKOSHII
Total number of polymer chains	6
Total formula weight	61857.48
Authors	Lam, S.Y.,Wong, K.B. (deposition date: 2008-11-25, release date: 2009-12-22, Last modification date: 2023-12-13)
Primary citation	Lam, S.Y.,Yeung, R.C.Y.,Yu, T.,Sze, K.,Wong, K.B. A Rigidifying Salt-Bridge Favors the Activity of Thermophilic Enzyme at High Temperatures at the Expense of Low-Temperature Activity. Plos Biol., 9:1027-, 2011 Cited by PubMed Abstract: Thermophilic enzymes are often less active than their mesophilic homologues at low temperatures. One hypothesis to explain this observation is that the extra stabilizing interactions increase the rigidity of thermophilic enzymes and hence reduce their activity. Here we employed a thermophilic acylphosphatase from Pyrococcus horikoshii and its homologous mesophilic acylphosphatase from human as a model to study how local rigidity of an active-site residue affects the enzymatic activity. PubMed: 21423654 DOI: 10.1371/JOURNAL.PBIO.1001027 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.4 Å)

Structure validation