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PDBsum entry 1n00

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protein ligands links
Membrane protein PDB id
1n00
Jmol
Contents
Protein chain
318 a.a. *
Ligands
SO4 ×3
Waters ×181
* Residue conservation analysis
PDB id:
1n00
Name: Membrane protein
Title: Annexin gh1 from cotton
Structure: Annexin gh1. Chain: a. Engineered: yes
Source: Gossypium hirsutum. Upland cotton. Organism_taxid: 3635. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.10Å     R-factor:   0.219     R-free:   0.280
Authors: A.Hofmann,D.P.Delmer,A.Wlodawer
Key ref:
A.Hofmann et al. (2003). The crystal structure of annexin Gh1 from Gossypium hirsutum reveals an unusual S3 cluster. Eur J Biochem, 270, 2557-2564. PubMed id: 12787021 DOI: 10.1046/j.1432-1033.2003.03612.x
Date:
10-Oct-02     Release date:   24-Jun-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P93157  (P93157_GOSHI) -  Annexin (Fragment)
Seq:
Struc:
315 a.a.
318 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     calcium-dependent phospholipid binding     3 terms  

 

 
DOI no: 10.1046/j.1432-1033.2003.03612.x Eur J Biochem 270:2557-2564 (2003)
PubMed id: 12787021  
 
 
The crystal structure of annexin Gh1 from Gossypium hirsutum reveals an unusual S3 cluster.
A.Hofmann, D.P.Delmer, A.Wlodawer.
 
  ABSTRACT  
 
The three-dimensional crystal structure of recombinant annexin Gh1 from Gossypium hirsutum (cotton fibre) has been determined and refined to the final R-factor of 0.219 at the resolution of 2.1 A. This plant annexin consists of the typical 'annexin fold' and is similar to the previously solved bell pepper annexin Anx24(Ca32), but significant differences are seen when compared to the structure of nonplant annexins. A comparison with the structure of the mammalian annexin AnxA5 indicates that canonical calcium binding is geometrically possible within the membrane loops in domains I and II of Anx(Gh1) in their present conformation. All plant annexins possess a conserved tryptophan residue in the AB loop of the first domain; this residue was found to adopt both a loop-in and a loop-out conformation in the bell pepper annexin Anx24(Ca32). In Anx(Gh1), the conserved tryptophan residue is in a surface-exposed position, half way between both conformations observed in Anx24(Ca32). The present structure reveals an unusual sulfur cluster formed by two cysteines and a methionine in domains II and III, respectively. While both cysteines adopt the reduced thiolate forms and are separated by a distance of about 5.5 A, the sulfur atom of the methionine residue is in their close vicinity and apparently interacts with both cysteine sulfur atoms. While the cysteine residues are conserved in at least five plant annexins and in several mammalian members of the annexin family of proteins, the methionine residue is conserved only in three plant proteins. Several of these annexins carrying the conserved residues have been implicated in oxidative stress response. We therefore hypothesize that the cysteine motif found in the present structure, or possibly even the entire sulfur cluster, forms the molecular basis for annexin function in oxidative stress response.
 
  Selected figure(s)  
 
Figure 2.
Fig. 2. The membrane binding loops. The IAB loops of Anx(Gh1) (A) and AnxA5 (B) are shown in the same view from the front. (C) and (D) show the IIAB loops of Anx(Gh1) and AnxA5, respectively, from the top (membrane-binding) side. The yellow ball indicates a calcium ion. Note that the IAB loop of Anx(Gh1) provides suitable environment for calcium binding. The IIAB loop, however, features a histidine residue occluding access to the binding site. A bidentate ligand required for canonical calcium binding is also missing.
Figure 3.
Fig. 3. The sulfur cluster. Spatial arrangement of the S[3] cluster formed by Met112, Cys116, and Cys243. The electron density shown was calculated as omit map and is contoured at 1.5 . Helices IIB and IIIE are shown as Ca traces. Inset: The distances between the individual sulfur atoms are given in Å.
 
  The above figures are reprinted by permission from the Federation of European Biochemical Societies: Eur J Biochem (2003, 270, 2557-2564) copyright 2003.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21083562 A.Laohavisit, and J.M.Davies (2011).
Annexins.
  New Phytol, 189, 40-53.  
  21348939 L.Zhou, J.Duan, X.M.Wang, H.M.Zhang, M.X.Duan, and J.Y.Liu (2011).
Characterization of a novel annexin gene from cotton (Gossypium hirsutum cv CRI 35) and antioxidative role of its recombinant protein.
  J Integr Plant Biol, 53, 347-357.  
  20215861 G.Clark, D.Konopka-Postupolska, J.Hennig, and S.Roux (2010).
Is annexin 1 a multifunctional protein during stress responses?
  Plant Signal Behav, 5, 303-307.  
20148350 K.Divya, S.K.Jami, and P.B.Kirti (2010).
Constitutive expression of mustard annexin, AnnBj1 enhances abiotic stress tolerance and fiber quality in cotton under stress.
  Plant Mol Biol, 73, 293-308.  
19885739 L.K.Wang, X.W.Niu, Y.H.Lv, T.Z.Zhang, and W.Z.Guo (2010).
Molecular cloning and localization of a novel cotton annexin gene expressed preferentially during fiber development.
  Mol Biol Rep, 37, 3327-3334.  
18441010 N.J.Hu, A.M.Yusof, A.Winter, A.Osman, A.K.Reeve, and A.Hofmann (2008).
The crystal structure of calcium-bound annexin Gh1 from Gossypium hirsutum and its implications for membrane binding mechanisms of plant annexins.
  J Biol Chem, 283, 18314-18322.
PDB code: 3brx
18447950 N.S.Hotte, and M.K.Deyholos (2008).
A flax fibre proteome: identification of proteins enriched in bast fibres.
  BMC Plant Biol, 8, 52.  
16978258 J.Bouzenzana, L.Pelosi, A.Briolay, J.Briolay, and V.Bulone (2006).
Identification of the first Oomycete annexin as a (1-->3)-beta-D-glucan synthase activator.
  Mol Microbiol, 62, 552-565.  
17058302 Y.Yao, Y.W.Yang, and J.Y.Liu (2006).
An efficient protein preparation for proteomic analysis of developing cotton fibers by 2-DE.
  Electrophoresis, 27, 4559-4569.  
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.