PDBsum entry 2jwt

Transcription

PDB id: 2jwt

Contents

Protein chain

61 a.a. *

* Residue conservation analysis

PDB id:

2jwt

Name:

Transcription

Title:

Solution structure of engrailed homeodomain wt

Structure:

Segmentation polarity homeobox protein engrailed. Chain: a. Fragment: homeobox domain. Engineered: yes

Source:

Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Gene: en. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

25 models

Authors:

T.L.Religa

Key ref:

T.L.Religa (2008). Comparison of multiple crystal structures with NMR data for engrailed homeodomain. J Biomol Nmr, 40, 189-202. PubMed id: 18274703

Date:

24-Oct-07 Release date: 01-Apr-08

Protein chain

P02836  (HMEN_DROME) -  Segmentation polarity homeobox protein engrailed from Drosophila melanogaster

Seq: 552 a.a.

Struc: 61 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

J Biomol Nmr 40:189-202 (2008)

PubMed id: 18274703

Comparison of multiple crystal structures with NMR data for engrailed homeodomain.

T.L.Religa.

ABSTRACT

Two methods are currently available to solve high resolution protein structures-X-ray crystallography and nuclear magnetic resonance (NMR). Both methods usually produce highly similar structures, but small differences between both solutions are always observed. Here the raw NMR data as well as the solved NMR structure were compared to the multiple crystal structures solved for the WT 60 residue three helix bundle engrailed homeodomain (EnHD) and single point mutants. There was excellent agreement between TALOS-predicted and crystal structure-observed dihedral angles and a good agreement for the (3) J(H ( N ) H ( alpha )) couplings for the multiple crystal structures. Around 1% of NOEs were violated for any crystal structure, but no NOE was inconsistent with all of the crystal structures. Violations usually occurred for surface residues or for residues for which multiple discreet conformations were observed between the crystal structures. Comparison of the disorder shown in the multiple crystal structures shows little correlation with dynamics under native conditions for this protein.