PDBsum entry 1lfs

Replication

PDB id

1lfs

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Contents

			Protein chain

					340 a.a.

Theoretical model

PDB id:

1lfs

Links
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Name:

Replication

Title:

Theoretical structure of replication factor c 36 kda subunit

Structure:

Replication factor c 36 kda subunit. Chain: a. Synonym: activator 1 36 kda subunit, rfc36

Source:

Homo sapiens. Human. Cellular_location: nucleus

Authors:

R.P.K.Surendra,T.Neelima,K.K.Kakarala

Key ref:

G.E.Norris et al. (1991). Molecular replacement solution of the structure of apolactoferrin, a protein displaying large-scale conformational change. Acta Crystallogr B, 47, 998. PubMed id: 1772635

Date:

12-Apr-02

Release date:

12-Jun-02

PROCHECK

	Headers

	References

Protein chain

P40937 (RFC5_HUMAN) - Replication factor C subunit 5

Seq: Struc:					340 a.a. 340 a.a.

Key:

PfamA domain

Secondary structure

	Acta Crystallogr B 47:998 (1991)
PubMed id: 1772635

Molecular replacement solution of the structure of apolactoferrin, a protein displaying large-scale conformational change.
G.E.Norris, B.F.Anderson, E.N.Baker.

ABSTRACT

The crystal structure of an orthorhombic form of human apolactoferrin (ApoLf) has been determined from 2.8 A diffractometer data by molecular replacement methods. A variety of search models derived from the diferric lactoferrin structure (Fe2Lf) were used to obtain a consistent solution to the rotation function. An R-factor search gave the correct translational solution and the model was refined by rigid-body least-squares refinement (program CORELS). Only three of the four domains were located correctly by this procedure, however; the fourth was finally placed correctly by rotating it manually onto three strands of electron density which were recognized as part of its central beta-sheet. The final model, refined by restrained least-squares methods to an R factor of 0.214 for data in the resolution range 10.0 to 2.8 A, shows a large domain movement in the N-terminal half of the molecule (a 54 degree rotation of domain N2) and smaller domain movements elsewhere, when compared with Fe2Lf. A feature of the crystal structure is that although the ApoLf and Fe2Lf unit cells appear very similar, their crystal packing and molecular structures are quite different.

Literature references that cite this PDB file's key reference

PubMed id

Reference

18433058

S.C.Flores, K.S.Keating, J.Painter, F.Morcos, K.Nguyen, E.A.Merritt, L.A.Kuhn, and M.B.Gerstein (2008).
HingeMaster: normal mode hinge prediction approach and integration of complementary predictors.

Proteins, 73, 299-319.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.