Protein sectors: evolutionary units of three-dimensional structure.


Abstract

Proteins display a hierarchy of structural features at primary, secondary, tertiary, and higher-order levels, an organization that guides our current understanding of their biological properties and evolutionary origins. Here, we reveal a structural organization distinct from this traditional hierarchy by statistical analysis of correlated evolution between amino acids. Applied to the S1A serine proteases, the analysis indicates a decomposition of the protein into three quasi-independent groups of correlated amino acids that we term "protein sectors." Each sector is physically connected in the tertiary structure, has a distinct functional role, and constitutes an independent mode of sequence divergence in the protein family. Functionally relevant sectors are evident in other protein families as well, suggesting that they may be general features of proteins. We propose that sectors represent a structural organization of proteins that reflects their evolutionary histories.

Submission Details

ID: k2fFYxka

Submitter: Connie Wang

Submission Date: Oct. 22, 2018, 12:21 p.m.

Version: 1

Publication Details
Halabi N;Rivoire O;Leibler S;Ranganathan R,Cell (2009) Protein sectors: evolutionary units of three-dimensional structure. PMID:19703402
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
1AMH 1997-06-17T00:00:00+0000 2.5 UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S)
1ANB 1994-12-21T00:00:00+0000 2.8 ANIONIC TRYPSIN MUTANT WITH SER 214 REPLACED BY GLU
1ANC 1994-12-21T00:00:00+0000 2.2 ANIONIC TRYPSIN MUTANT WITH SER 214 REPLACED BY LYS
1AND 1994-12-21T00:00:00+0000 2.3 ANIONIC TRYPSIN MUTANT WITH ARG 96 REPLACED BY HIS
1ANE 1994-12-21T00:00:00+0000 2.2 ANIONIC TRYPSIN WILD TYPE
1BRA 1992-12-17T00:00:00+0000 2.2 RELOCATING A NEGATIVE CHARGE IN THE BINDING POCKET OF TRYPSIN
1BRB 1992-12-17T00:00:00+0000 2.1 CRYSTAL STRUCTURES OF RAT ANIONIC TRYPSIN COMPLEXED WITH THE PROTEIN INHIBITORS APPI AND BPTI
1BRC 1992-12-17T00:00:00+0000 2.5 RELOCATING A NEGATIVE CHARGE IN THE BINDING POCKET OF TRYPSIN
1CO7 1999-06-07T00:00:00+0000 1.9 R117H mutant rat anionic trypsin complexed with bovine pancreatic trypsin inhibitor (BPTI)
1DPO 1997-03-31T00:00:00+0000 1.59 STRUCTURE OF RAT TRYPSIN

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Anionic trypsin-2 P00763 TRY2_RAT