PDBsum entry 2qb0

Hydrolase regulator

PDB id: 2qb0

Contents

Protein chains

77 a.a. *

241 a.a. *

Metals

_MN ×5

Waters ×147

* Residue conservation analysis

PDB id:

2qb0

Name:

Hydrolase regulator

Title:

Structure of the 2tel crystallization module fused to t4 lysozyme with an ala-gly-pro linker.

Structure:

Transcription factor etv6. Chain: a, c. Synonym: ets translocation variant 6,ets-related protein tel1,tel. Engineered: yes. Mutation: yes. Transcription factor etv6,endolysin. Chain: b, d. Synonym: ets translocation variant 6,ets-related protein tel1,tel, lysis protein,lysozyme,muramidase.

Source:

Homo sapiens. Organism_taxid: 9606. Gene: etv6, tel, tel1. Expressed in: escherichia coli. Expression_system_taxid: 562. Human. Expression_system_taxid: 562

Resolution:

2.56Å R-factor: 0.213 R-free: 0.252

Authors:

S.Nauli,J.U.Bowie

Key ref:

S.Nauli et al. (2007). Polymer-driven crystallization. Protein Sci, 16, 2542-2551. PubMed id: 17962407 DOI: 10.1110/ps.073074207

Date:

15-Jun-07 Release date: 14-Oct-08

Protein chains

P41212  (ETV6_HUMAN) -  Transcription factor ETV6 from Homo sapiens

Seq: 452 a.a.

Struc: 77 a.a.*

Protein chains

P00720  (ENLYS_BPT4) -  Endolysin from Enterobacteria phage T4

Seq: 164 a.a.

Struc: 241 a.a.*

* PDB and UniProt seqs differ at 8 residue positions (black crosses)

Enzyme reactions

• Enzyme class 2: Chains A, C: E.C.?
• Enzyme class 3: Chains B, D: E.C.3.2.1.17 - lysozyme.
• Reaction: Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

DOI no: 10.1110/ps.073074207

Protein Sci 16:2542-2551 (2007)

PubMed id: 17962407

Polymer-driven crystallization.

S.Nauli, S.Farr, Y.J.Lee, H.Y.Kim, S.Faham, J.U.Bowie.

ABSTRACT

Obtaining well-diffracting crystals of macromolecules remains a significant barrier to structure determination. Here we propose and test a new approach to crystallization, in which the crystallization target is fused to a polymerizing protein module, so that polymer formation drives crystallization of the target. We test the approach using a polymerization module called 2TEL, which consists of two tandem sterile alpha motif (SAM) domains from the protein translocation Ets leukemia (TEL). The 2TEL module is engineered to polymerize as the pH is lowered, which allows the subtle modulation of polymerization needed for crystal formation. We show that the 2TEL module can drive the crystallization of 11 soluble proteins, including three that resisted prior crystallization attempts. In addition, the 2TEL module crystallizes in the presence of various detergents, suggesting that it might facilitate membrane protein crystallization. The crystal structures of two fusion proteins show that the TELSAM polymer is responsible for the majority of contacts in the crystal lattice. The results suggest that biological polymers could be designed as crystallization modules.

Selected figure(s)

Figure 4.
Figure 4. Crystal structures and packing of the 2TEL module (sticks model) fused to T4 lysozyme (ribbon diagram) viewed down the

The above figure is reprinted by permission from the Protein Society: Protein Sci (2007, 16, 2542-2551) copyright 2007.

Figure was selected by the author.

Author's comment

The figure shows the crystal contacts observed for a fusion protein containing the 2TEL crystallization module and T4-lysozyme.