PDBsum entry 1xhh

Unknown function

PDB id: 1xhh

Contents

Protein chain

91 a.a. *

* Residue conservation analysis

PDB id:

1xhh

Name:

Unknown function

Title:

Solution structure of porcine beta-microseminoprotein

Structure:

Beta-microseminoprotein. Chain: a. Engineered: yes

Source:

Sus scrofa. Pig. Organism_taxid: 9823. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

I.Wang,Y.C.Lou,K.P.Wu,S.H.Wu,W.C.Chang,C.Chen

Key ref:

I.Wang et al. (2005). Novel solution structure of porcine beta-microseminoprotein. J Mol Biol, 346, 1071-1082. PubMed id: 15701518 DOI: 10.1016/j.jmb.2004.12.029

Date:

20-Sep-04 Release date: 20-Mar-05

Protein chain

O02826  (MSMB_PIG) -  Beta-microseminoprotein from Sus scrofa

Seq: 111 a.a.

Struc: 91 a.a.*

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

DOI no: 10.1016/j.jmb.2004.12.029

J Mol Biol 346:1071-1082 (2005)

PubMed id: 15701518

Novel solution structure of porcine beta-microseminoprotein.

I.Wang, Y.C.Lou, K.P.Wu, S.H.Wu, W.C.Chang, C.Chen.

ABSTRACT

A number of beta-microseminoproteins (MSPs) have been identified from different species. MSPs are all non-glycosylated and disulfide bond-rich, but show a relatively low level of conservation. Although all Cys residues are conserved, our previous study showed that the disulfide bond pairings differ in porcine and ostrich MSPs. Despite the variety of biological functions that have been suggested for MSPs, their real function is still poorly understood. Furthermore, no 3D structure has been reported for any MSP, so the determination of the structure and function of MSPs is an interesting and important task. In the present study, we determined the 3D solution structure of porcine MSP on the basis of 1018 restraints. The ensemble of 20 NMR structures was well defined, with average root-mean-square deviations of 0.83(+/-0.16) A for the backbone atoms and 1.37(+/-0.17) A for heavy-atoms in residues 2-90. The 3D structure showed that porcine MSP is clearly composed of two domains, an N-terminal domain consisting of one double-stranded and one four-stranded antiparallel beta-sheet, and a C-terminal domain consisting of two double-stranded antiparallel beta-sheet. The orientation of the two domains was derived mainly on the basis of long-range NOEs and verified using residual dipolar coupling data. No inter-domain hydrophobic interaction or H-bonding was detected. However, a number of charged residues were found in close proximity between the domains, indicating that electrostatic interaction may be the key factor for the orientation of the two domains. This is the first report of a 3D structure for any MSP. In addition, structural comparison based on distance matrix alignment (DALI), class architecture topology and homologous superfamily (CATH) and combinatorial extension (CE) methods revealed that porcine MSP has a novel structure with a new fold providing valuable information for future structural studies on other MSPs and for understanding their biological functions.

Selected figure(s)

Figure 5.
Figure 5. Surface structure of porcine MSP displayed as a 180° rotation with positive and negative charges shown in blue and red, respectively.

Figure 8.
Figure 8. Comparison of the 3D structures of porcine MSP and a fibronectin fragment (PDB number 1E8B). Similar regions in the two structures are shown in red and the ranges of each region used for comparison are labeled using different color codes.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2005, 346, 1071-1082) copyright 2005.

Figures were selected by an automated process.