PDBsum entry 2n1a

Transcription

PDB id: 2n1a

Contents

Protein chains

103 a.a.

53 a.a.

Metals

_ZN ×2

PDB id:

2n1a

Name:

Transcription

Title:

Docked structure between sumo1 and zz-domain from cbp

Structure:

Small ubiquitin-related modifier 1. Chain: a. Synonym: sumo-1, gap-modifying protein 1, gmp1, smt3 homolog 3, sentrin, ubiquitin-homology domain protein pic1, ubiquitin-like protein smt3c, smt3c, ubiquitin-like protein ubl1. Engineered: yes. Creb-binding protein. Chain: b. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ok/sw-cl.43, smt3c, smt3h3, sumo1, ubl1. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: cbp, crebbp.

NMR struc:

6 models

Authors:

C.Diehl

Key ref:

C.Diehl et al. (2016). Structural Analysis of a Complex between Small Ubiquitin-like Modifier 1 (SUMO1) and the ZZ Domain of CREB-binding Protein (CBP/p300) Reveals a New Interaction Surface on SUMO. J Biol Chem, 291, 12658-12672. PubMed id: 27129204 DOI: 10.1074/jbc.M115.711325

Date:

26-Mar-15 Release date: 04-May-16

Protein chain

P63165  (SUMO1_HUMAN) -  Small ubiquitin-related modifier 1 from Homo sapiens

Seq: 101 a.a.

Struc: 103 a.a.

Protein chain

Q92793  (CBP_HUMAN) -  CREB-binding protein from Homo sapiens

Seq: 2442 a.a.

Struc: 53 a.a.

Enzyme reactions

• Enzyme class 1: Chain A: E.C.?
• Enzyme class 2: Chain B: E.C.2.3.1.- - ?????
• Enzyme class 3: Chain B: E.C.2.3.1.48 - histone acetyltransferase.
• Reaction: L-lysyl-[protein] + acetyl-CoA = N₆-acetyl-L-lysyl-[protein] + CoA + H⁺

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.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1074/jbc.M115.711325

J Biol Chem 291:12658-12672 (2016)

PubMed id: 27129204

Structural Analysis of a Complex between Small Ubiquitin-like Modifier 1 (SUMO1) and the ZZ Domain of CREB-binding Protein (CBP/p300) Reveals a New Interaction Surface on SUMO.

C.Diehl, M.Akke, S.Bekker-Jensen, N.Mailand, W.Streicher, M.Wikström.

ABSTRACT

We have recently discovered that the ZZ zinc finger domain represents a novel small ubiquitin-like modifier (SUMO) binding motif. In this study we identify the binding epitopes in the ZZ domain of CBP (CREB-binding protein) and SUMO1 using NMR spectroscopy. The binding site on SUMO1 represents a unique epitope for SUMO interaction spatially opposite to that observed for canonical SUMO interaction motifs (SIMs). HADDOCK docking simulations using chemical shift perturbations and residual dipolar couplings was employed to obtain a structural model for the ZZ domain-SUMO1 complex. Isothermal titration calorimetry experiments support this model by showing that the mutation of key residues in the binding site abolishes binding and that SUMO1 can simultaneously and non-cooperatively bind both the ZZ domain and a canonical SIM motif. The binding dynamics of SUMO1 was further characterized using (15)N Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersions, which define the off rates for the ZZ domain and SIM motif and show that the dynamic binding process has different characteristics for the two cases. Furthermore, in the absence of bound ligands SUMO1 transiently samples a high energy conformation, which might be involved in ligand binding.