PDBsum entry 2mbb

Transferase, signaling protein

PDB id: 2mbb

Contents

Protein chains

38 a.a.

76 a.a.

PDB id:

2mbb

Name:

Transferase, signaling protein

Title:

Solution structure of the human polymerase iota ubm1-ubiquitin complex

Structure:

Immunoglobulin g-binding protein g/DNA polymerase iota fusion protein. Chain: a. Fragment: unp p06654 residues 229-282, unp q9una4 residues 516-555. Engineered: yes. Polyubiquitin-b. Chain: b. Fragment: unp p0cg47 residues 1-76. Synonym: ubiquitin.

Source:

Streptococcus sp. 'Group g', homo sapiens. Organism_taxid: 1320,9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human. Organism_taxid: 9606. Gene: ubb.

NMR struc:

20 models

Authors:

S.Wang,P.Zhou

Key ref:

S.Wang and P.Zhou (2014). Sparsely-sampled, high-resolution 4-D omit spectra for detection and assignment of intermolecular NOEs of protein complexes. J Biomol Nmr, 59, 51-56. PubMed id: 24789524 DOI: 10.1007/s10858-014-9834-2

Date:

29-Jul-13 Release date: 04-Jun-14

Protein chain

P06654  (SPG1_STRSG) -  Immunoglobulin G-binding protein G from Streptococcus sp. group G

Seq: 448 a.a.

Struc: 38 a.a.*

Protein chain

Q9UNA4  (POLI_HUMAN) -  DNA polymerase iota from Homo sapiens

Seq: 740 a.a.

Struc: 38 a.a.*

Protein chain

P0CG47  (UBB_HUMAN) -  Polyubiquitin-B from Homo sapiens

Seq: 229 a.a.

Struc: 76 a.a.

* PDB and UniProt seqs differ at 28 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chain A: E.C.2.7.7.7 - DNA-directed Dna polymerase.
• Reaction: DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate

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

Added reference

DOI no: 10.1007/s10858-014-9834-2

J Biomol Nmr 59:51-56 (2014)

PubMed id: 24789524

Sparsely-sampled, high-resolution 4-D omit spectra for detection and assignment of intermolecular NOEs of protein complexes.

S.Wang, P.Zhou.

ABSTRACT

Unambiguous detection and assignment of intermolecular NOEs are essential for structure determination of protein complexes by NMR. Such information has traditionally been obtained with 3-D half-filtered experiments, where scalar coupling-based purging of intramolecular signals allows for selective detection of intermolecular NOEs. However, due to the large variation of (1)JHC scalar couplings and limited chemical shift dispersion in the indirect proton dimension, it is difficult to obtain reliable and complete assignments of interfacial NOEs. Here, we demonstrate a strategy that combines selective labeling and high-resolution 4-D NOE spectroscopy with sparse sampling for reliable identification and assignment of intermolecular NOEs. Spectral subtraction of component-labeled complexes from a uniformly-labeled protein complex yields an "omit" spectrum containing positive intermolecular NOEs with little signal degeneracy. Such a strategy can be broadly applied to unbiased detection, assignment and presentation of intermolecular NOEs of protein complexes.