PDBsum entry: 1sqw

Unknown function

PDB id: 1sqw

Contents

Protein chain

176 a.a. *

Waters ×131

* Residue conservation analysis

PDB id:

1sqw

Name:

Unknown function

Title:

Crystal structure of kd93, a novel protein expressed in the human pro

Structure:

Saccharomyces cerevisiae nip7p homolog. Chain: a. Engineered: yes. Other_details: novel protein expressed in human hematopoietic stem/progenitor cells

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: novel gene. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.90Å R-factor: 0.225 R-free: 0.261

Authors:

J.F.Liu,X.Q.Wang,Z.X.Wang,J.R.Chen,T.Jiang,X.M.An,W.R.Chan, D.C.Liang

Key ref:

J.F.Liu et al. (2004). Crystal structure of KD93, a novel protein expressed in human hematopoietic stem/progenitor cells. J Struct Biol, 148, 370-374. PubMed id: 15522784 DOI: 10.1016/j.jsb.2004.06.010

Date:

19-Mar-04 Release date: 22-Mar-05

Protein chain

Q9Y221  (NIP7_HUMAN) -  60S ribosome subunit biogenesis protein NIP7 homolog

Seq: 180 a.a.

Struc: 176 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: nucleus (2 terms)
• Biological process: ribosome biogenesis (2 terms)
• Biochemical function: protein binding (2 terms)

DOI no: 10.1016/j.jsb.2004.06.010

J Struct Biol 148:370-374 (2004)

PubMed id: 15522784

Crystal structure of KD93, a novel protein expressed in human hematopoietic stem/progenitor cells.

J.F.Liu, X.Q.Wang, Z.X.Wang, J.R.Chen, T.Jiang, X.M.An, W.R.Chang, D.C.Liang.

ABSTRACT

The crystal structure of a novel hypothetical protein, KD93, expressed in human hematopoietic stem/progenitor cells, was determined at 1.9A resolution using the multiple-wavelength anomalous dispersion (MAD) method. The protein KD93, which is encoded by the open reading frame HSPC031, is a NIP7 homologue and belongs to the UPF0113 family. The structural and functional information for the group of homologues has not yet been determined. Crystallographic analysis revealed that the overall fold of KD93 consists of two interlinked alpha/beta domains. Structure-based homology analysis with DALI revealed that the C domain of KD93 matches the PUA domain of some RNA modification enzymes, especially that of archaeosine tRNA-ribosyltransferase (ArcTGT), which suggests that its possible molecular function is related to RNA binding. The difference between the RNA binding regions of KD93 and ArcTGT in amino acid constitution and surface electrostatic potential indicate that they may have different RNA binding modes. The N domain of KD93 is a unique structure with no obvious similarity to other proteins with known three-dimensional structures. The high-resolution structure of KD93 provides a first view of a member of the family of hypothetical proteins. And the structure provides a framework to deduce and assay the molecular function of other proteins of the UPF0113 family.