Hydrolase

PDB id

2ane

Contents

			Protein chains

					(+ 2 more) 110 a.a. *

			Waters ×593

* Residue conservation analysis

PDB id:

2ane

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Name:

Hydrolase

Title:

Crystal structure of n-terminal domain of e.Coli lon protease

Structure:

Atp-dependent protease la. Chain: a, b, c, d, e, f, g, h. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Gene: lon, capr, deg, lopa, muc. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.03Å

R-factor:

0.212

R-free:

0.268

Authors:

M.Li,F.Rasulova,E.E.Melnikov,T.V.Rotanova,A.Gustchina, M.R.Maurizi,A.Wlodawer

Key ref:

M.Li et al. (2005). Crystal structure of the N-terminal domain of E. coli Lon protease. Protein Sci, 14, 2895-2900. PubMed id: 16199667 DOI: 10.1110/ps.051736805

Date:

11-Aug-05

Release date:

01-Nov-05

PROCHECK

	Headers

	References

Protein chains

P0A9M0 (LON_ECOLI) - Lon protease

Seq: Struc:

Seq: Struc:					784 a.a. 110 a.a.

Key:

PfamA domain

Secondary structure



		Enzyme reactions

Enzyme class:

E.C.3.4.21.53 - Endopeptidase La.

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

Reaction:

Hydrolysis of large proteins such as globin, casein and denaturated serum albumin, in presence of ATP.



		Gene Ontology (GO) functional annotation

Biological process	proteolysis	1 term
Biochemical function	ATP-dependent peptidase activity	1 term

DOI no: 10.1110/ps.051736805	Protein Sci 14:2895-2900 (2005)
PubMed id: 16199667

Crystal structure of the N-terminal domain of E. coli Lon protease.
M.Li, F.Rasulova, E.E.Melnikov, T.V.Rotanova, A.Gustchina, M.R.Maurizi, A.Wlodawer.

ABSTRACT

We report here the first crystal structure of the N-terminal domain of an A-type Lon protease. Lon proteases are ubiquitous, multidomain, ATP-dependent enzymes with both highly specific and non-specific protein binding, unfolding, and degrading activities. We expressed and purified a stable, monomeric 119-amino acid N-terminal subdomain of the Escherichia coli A-type Lon protease and code 2ANE). The structure was solved in two crystal forms, yielding 14 independent views. The domain exhibits a unique fold consisting primarily of three twisted beta-sheets and a single long alpha-helix. Analysis of recent PDB depositions identified a similar fold in BPP1347 (PDB code 1ZBO), a 203-amino acid protein of unknown function from Bordetella parapertussis, crystallized as part of a structural genomics effort. BPP1347 shares sequence homology with Lon N-domains and with a family of other independently expressed proteins of unknown functions. We postulate that, as is the case in Lon proteases, this structural domain represents a general protein and polypeptide interaction domain.

Selected figure(s)



	Figure 1. Figure 1. Crystal structure of the N119 domain of E. coli Lon and its comparison with the structure of the hypothetical protein BPP1347. (A) Stereo view of LonN119 showing the elements of the secondary structure colored green for strands, blue for helices, and brown for coils. (B) Superposition of LonN119 (green) and B. parapertussis BPP1347 (gray).

Figure was selected by the author.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20130685

J.Thomas, J.Fishovitz, and I.Lee (2010).
Utilization of positional isotope exchange experiments to evaluate reversibility of ATP hydrolysis catalyzed by Escherichia coli Lon protease.

Biochem Cell Biol, 88, 119-128.

20693685

M.Li, A.Gustchina, F.S.Rasulova, E.E.Melnikov, M.R.Maurizi, T.V.Rotanova, Z.Dauter, and A.Wlodawer (2010).
Structure of the N-terminal fragment of Escherichia coli Lon protease.

Acta Crystallogr D Biol Crystallogr, 66, 865-873.

PDB code:

3ljc

20834233

S.S.Cha, Y.J.An, C.R.Lee, H.S.Lee, Y.G.Kim, S.J.Kim, K.K.Kwon, G.M.De Donatis, J.H.Lee, M.R.Maurizi, and S.G.Kang (2010).
Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber.

EMBO J, 29, 3520-3530.

19154314

N.L.Taylor, and A.H.Millar (2009).
Long bugs to short plants--the Lon protease in protein stability and thermotolerance.

New Phytol, 181, 505-508.

18446870

B.Friguet, A.L.Bulteau, and I.Petropoulos (2008).
Mitochondrial protein quality control: implications in ageing.

Biotechnol J, 3, 757-764.

18359303

I.Lee, and C.K.Suzuki (2008).
Functional mechanics of the ATP-dependent Lon protease- lessons from endogenous protein and synthetic peptide substrates.

Biochim Biophys Acta, 1784, 727-735.

18441029

M.Chruszcz, A.Wlodawer, and W.Minor (2008).
Determination of protein structures--a series of fortunate events.

Biophys J, 95, 1-9.

PDB code:

3pzw

16584195

D.Vineyard, J.Patterson-Ward, and I.Lee (2006).
Single-turnover kinetic experiments confirm the existence of high- and low-affinity ATPase sites in Escherichia coli Lon protease.

Biochemistry, 45, 4602-4610.

16511295

T.Arakaki, I.Le Trong, E.Phizicky, E.Quartley, G.DeTitta, J.Luft, A.Lauricella, L.Anderson, O.Kalyuzhniy, E.Worthey, P.J.Myler, D.Kim, D.Baker, W.G.Hol, and E.A.Merritt (2006).
Structure of Lmaj006129AAA, a hypothetical protein from Leishmania major.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 175-179.

PDB code:

2ar1

16877706

T.V.Rotanova, I.Botos, E.E.Melnikov, F.Rasulova, A.Gustchina, M.R.Maurizi, and A.Wlodawer (2006).
Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains.

Protein Sci, 15, 1815-1828.

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 code is shown on the right.