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2qzp

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Crystal structure of mutation of an acylptide hydrolase/esterase from Aeropyrum pernix K1

Structural highlights

2qzp is a 2 chain structure with sequence from Aeropyrum pernix. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.7Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

APEH_AERPE This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Acylpeptide hydrolase (APH) catalyzes the N-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids. The crystal structure of recombinant APH from the thermophilic archaeon Aeropyrum pernix K1 (apAPH) was reported recently to be at a resolution of 2.1 Angstrom; using X-ray diffraction. A truncated mutant of apAPH that lacks the first short alpha-helix at the N-terminal, apAPH-delta(1-21), was cloned, expressed, characterized and crystallized. Data from biochemical experiments indicate that the optimum temperature of apAPH is decreased by 15 degrees C with the deletion of the N-terminal alpha-helix. However, the enzyme activity at the optimal temperature does not change. It suggests that this N-terminal alpha-helix is essential for thermostability. Here, the crystal structure of apAPH-delta(1-21) has been determined by molecular replacement to 2.5 Angstrom;. A comparison between the two structures suggests a difference in thermostability, and it can be concluded that by adding or deleting a linking structure (located over different domains), the stability or even the activity of an enzyme can be modified.

Expression, purification and crystal structure of a truncated acylpeptide hydrolase from Aeropyrum pernix K1.,Zhang HF, Zheng BS, Peng Y, Lou ZY, Feng Y, Rao ZH Acta Biochim Biophys Sin (Shanghai). 2005 Sep;37(9):613-7. doi: , 10.1111/j.1745-7270.2005.00085.x. PMID:16143816^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zhang HF, Zheng BS, Peng Y, Lou ZY, Feng Y, Rao ZH. Expression, purification and crystal structure of a truncated acylpeptide hydrolase from Aeropyrum pernix K1. Acta Biochim Biophys Sin (Shanghai). 2005 Sep;37(9):613-7. PMID:16143816 doi:10.1111/j.1745-7270.2005.00085.x