2jyp

From Proteopedia

Coordinates for lowest energy structure of Aragonite protein-7, C-terminal domain

Structural highlights

2jyp is a 1 chain structure with sequence from Haliotis rufescens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 1 model
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

The RING or Really Interesting New Gene represents a family of eukaryotic sequences that bind Zn (II) ions and participate in intracellular processes involving protein-protein interaction. Although found in over 400 different proteins, very little is known regarding the structure-function properties of these domains because of the aggregation problems associated with RING sequences. To augment this data set, we report an unusual 36 AA C-terminal sequence of an extracellular matrix mollusk shell protein, AP7, that exhibits partial homology to the RING family. This Cys, His-containing sequence, termed AP7C, binds Zn (II) and other multivalent ions, but does not utilize a tetracoordinate complexation scheme for binding such as that found in Zn (II) finger polypeptides. Moreover, unlike Zn (II) finger and RING domains, this 36 AA can fold into a relatively stable structure in the absence of Zn (II). This folded structure consists of three short helical segments (A, B, and C), with segments A and B separated by a 4 AA type I beta-turn region and segments B and C separated by a 7 AA loop-like region. Interestingly, the putative RING-like region, -RRPFHECALCYSI-, experiences slow conformational exchange between two structural states in solution, most likely in response to imido ring interconversion at P8 and P21. Poisson-Boltzmann solvation calculations reveal that the AP7C molecular surface possesses a cationic region near its N-terminus, which lies adjacent to the 30 AA mineral modification domain in the AP7 protein. Given that the AP7C sequence does not influence mineralization, it is probable that this cationic pseudo-RING region is utilized by the AP7 protein for other tasks such as protein-protein interaction within the mollusk shell matrix.

Identification and Structural Characterization of an Unusual RING-Like Sequence within an Extracellular Biomineralization Protein, AP7.,Collino S, Kim IW, Evans JS Biochemistry. 2008 Mar 25;47(12):3745-55. Epub 2008 Feb 26. PMID:18298090^[1]

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

References

↑ Collino S, Kim IW, Evans JS. Identification and Structural Characterization of an Unusual RING-Like Sequence within an Extracellular Biomineralization Protein, AP7. Biochemistry. 2008 Mar 25;47(12):3745-55. Epub 2008 Feb 26. PMID:18298090 doi:10.1021/bi701949p