PDBsum entry 1bo9

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Metal transport PDB id
Protein chain
73 a.a. *
* Residue conservation analysis

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Key reference
Title Nmr solution structure of domain 1 of human annexin i shows an autonomous folding unit.
Authors J.Gao, Y.Li, H.Yan.
Ref. J Biol Chem, 1999, 274, 2971-2977. [DOI no: 10.1074/jbc.274.5.2971]
PubMed id 9915835
Annexins are excellent models for studying the folding mechanisms of multidomain proteins because they have four-eight homologous helical domains with low identity in sequence but high similarity in folding. The structure of an isolated domain 1 of human annexin I has been determined by NMR spectroscopy. The sequential assignments of the 1H, 13C, and 15N resonances of the isolated domain 1 were established by multinuclear, multidimensional NMR spectroscopy. The solution structure of the isolated domain 1 was derived from 1,099 experimental NMR restraints using a hybrid distance geometry-simulated annealing protocol. The root mean square deviation of the ensemble of 20 refined conformers that represent the structure from the mean coordinate set derived from them was 0. 57 +/- 0.14 A and 1.11 +/- 0.19 A for the backbone atoms and all heavy atoms, respectively. The NMR structure of the isolated domain 1 could be superimposed with a root mean square deviation of 1.36 A for all backbone atoms with the corresponding part of the crystal structure of a truncated human annexin I containing all four domains, indicating that the structure of the isolated domain 1 is highly similar to that when it folded together with the other three domains. The result suggests that in contrast to isolated domain 2, which is largely unfolded in solution, isolated domain 1 constitutes an autonomous folding unit and interdomain interactions may play critical roles in the folding of annexin I.
Figure 2.
Fig. 2. 15N-1H HSQC spectrum of domain 1 of human annexin I. Sequential assignments are indicated with one-letter amino acid codes and residue numbers. Pairs of cross-peaks resulting from the side chain NH[2] groups of asparagine and glutamine residues are connected by horizontal lines. The amino acid numbering is according to the isolated domain 1 with residue 1 corresponding to residue 14 in the crystal structure numbering.
Figure 5.
Fig. 5. The hydrophobic core structure of domain 2 and the interface between domains 2 and 4. The drawing is based on the x-ray structure of the truncated human annexin I containing four domains (18). The main-chains of domain 2 and domain 4 (partial) are represented by blue and cyan ribbons, respectively. The residues involved in the nonnative cap and the cluster of acidic residues as well as Arg-117 in domain 2 are shown in magenta. The residues within 5 Å distance of Leu-96 are shown in yellow, and other core residues are in gray. The residues of domain 4 are in green. Hydrogen bonds are indicated by dotted lines. The amino acid numbering is according to the crystal structure of the truncated annexin I.
The above figures are reprinted by permission from the ASBMB: J Biol Chem (1999, 274, 2971-2977) copyright 1999.
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