PDBsum entry 1rtq

Hydrolase

PDB id

1rtq

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Contents

			Protein chain

					291 a.a. *

			Ligands

					SCN ×2

			Metals

					_NA ×3


					_ZN ×2

			Waters ×324

* Residue conservation analysis

PDB id:

1rtq

Links

Name:

Hydrolase

Title:

The 0.95 angstrom resolution crystal structure of the aminopeptidase from aeromonas proteolytica

Structure:

Bacterial leucyl aminopeptidase. Chain: a. Fragment: aminopeptidase. Engineered: yes

Source:

Vibrio proteolyticus. Organism_taxid: 671. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Dimer (from PQS)

Resolution:

0.95Å

R-factor:

0.135

R-free:

0.151

Authors:

W.Desmarais,D.L.Bienvenue,B.P.Krzysztof,R.C.Holz,G.A.Petsko,D.Ringe

Key ref:

W.Desmarais et al. (2006). The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica. J Biol Inorg Chem, 11, 398-408. PubMed id: 16596389

Date:

10-Dec-03

Release date:

10-Feb-04

PROCHECK

	Headers

	References

Protein chain

Q01693 (AMPX_VIBPR) - Bacterial leucyl aminopeptidase from Vibrio proteolyticus

Seq: Struc:					504 a.a. 291 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.3.4.11.10 - bacterial leucyl aminopeptidase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.

Cofactor:

Zn(2+)

	J Biol Inorg Chem 11:398-408 (2006)
PubMed id: 16596389

The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica.
W.Desmarais, D.L.Bienvenue, K.P.Bzymek, G.A.Petsko, D.Ringe, R.C.Holz.

ABSTRACT

The aminopeptidase from Aeromonas proteolytica (AAP) contains two zinc ions in the active site and catalyzes the degradation of peptides. Herein we report the crystal structures of AAP at 0.95-A resolution at neutral pH and at 1.24-A resolution at low pH. The combination of these structures allowed the precise modeling of atomic positions, the identification of the metal bridging oxygen species, and insight into the physical properties of the metal ions. On the basis of these structures, a new putative catalytic mechanism is proposed for AAP that is likely relevant to all binuclear metalloproteases.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20138056

B.P.Nocek, D.M.Gillner, Y.Fan, R.C.Holz, and A.Joachimiak (2010).
Structural basis for catalysis by the mono- and dimetalated forms of the dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase.

J Mol Biol, 397, 617-626.

PDB codes:

3ic1 3isz

18781344

C.Y.Huang, C.C.Hsu, M.C.Chen, and Y.S.Yang (2009).
Effect of metal binding and posttranslational lysine carboxylation on the activity of recombinant hydantoinase.

J Biol Inorg Chem, 14, 111-121.

19691327

J.A.Larrabee, W.R.Johnson, and A.S.Volwiler (2009).
Magnetic circular dichroism study of a dicobalt(II) complex with mixed 5- and 6-coordination: a spectroscopic model for dicobalt(II) hydrolases.

Inorg Chem, 48, 8822-8829.

19233285

M.Hartley, W.Yong, and B.Bennett (2009).
Heterologous expression and purification of Vibrio proteolyticus (Aeromonas proteolytica) aminopeptidase: a rapid protocol.

Protein Expr Purif, 66, 91.

PDB code:

3fh4

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.