1ohg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==Overview==
==Overview==
-
The HK97 bacteriophage capsid is a unique example of macromolecular, catenanes: interlocked rings of covalently attached protein subunits. The, chain mail organization of the subunits stabilizes a particle in which the, maximum thickness of the protein shell is 18A and the maximum diameter is, 550A. The electron density has the appearance of a balloon illustrating, the extraordinary strength conferred by the unique subunit organization., The refined structure shows novel qualities of the HK97 shell protein, gp5, that, together with the protease gp4, guides the assembly and maturation, of the virion. Although gp5 forms hexamers and pentamers and the subunits, exist in different structural environments, the tertiary structures of the, seven protein molecules in the viral asymmetric unit are closely similar., The interactions of the subunits in the shell are exceptionally complex, with each subunit interacting with nine other subunits. The interactions, of the N-terminus released after gp5 cleavage appear important for, organization of the loops that become crosslinked to the core of a, neighboring subunit at the maturation. A comparison with a model of the, Prohead II structure revealed that the surfaces of non-covalent contact, between the monomers that build up hexamers/pentamers are completely, redefined during maturation.
+
The HK97 bacteriophage capsid is a unique example of macromolecular catenanes: interlocked rings of covalently attached protein subunits. The chain mail organization of the subunits stabilizes a particle in which the maximum thickness of the protein shell is 18A and the maximum diameter is 550A. The electron density has the appearance of a balloon illustrating the extraordinary strength conferred by the unique subunit organization. The refined structure shows novel qualities of the HK97 shell protein, gp5 that, together with the protease gp4, guides the assembly and maturation of the virion. Although gp5 forms hexamers and pentamers and the subunits exist in different structural environments, the tertiary structures of the seven protein molecules in the viral asymmetric unit are closely similar. The interactions of the subunits in the shell are exceptionally complex with each subunit interacting with nine other subunits. The interactions of the N-terminus released after gp5 cleavage appear important for organization of the loops that become crosslinked to the core of a neighboring subunit at the maturation. A comparison with a model of the Prohead II structure revealed that the surfaces of non-covalent contact between the monomers that build up hexamers/pentamers are completely redefined during maturation.
==About this Structure==
==About this Structure==
-
1OHG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_hk620 Enterobacteria phage hk620] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1FH6. The following page contains interesting information on the relation of 1OHG with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb93_1.html Citrate Synthase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OHG OCA].
+
1OHG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_hk620 Enterobacteria phage hk620] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1FH6. The following page contains interesting information on the relation of 1OHG with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb93_1.html Citrate Synthase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OHG OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Enterobacteria phage hk620]]
[[Category: Enterobacteria phage hk620]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Duda, R.L.]]
+
[[Category: Duda, R L.]]
[[Category: Helgstrand, C.]]
[[Category: Helgstrand, C.]]
-
[[Category: Hendrix, R.W.]]
+
[[Category: Hendrix, R W.]]
-
[[Category: Johnson, J.E.]]
+
[[Category: Johnson, J E.]]
[[Category: Liljas, L.]]
[[Category: Liljas, L.]]
-
[[Category: Wikoff, W.R.]]
+
[[Category: Wikoff, W R.]]
[[Category: CL]]
[[Category: CL]]
[[Category: SO4]]
[[Category: SO4]]
Line 29: Line 29:
[[Category: virus/viral protein]]
[[Category: virus/viral protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:34:18 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:17:46 2008''

Revision as of 12:17, 21 February 2008


1ohg, resolution 3.45Å

Drag the structure with the mouse to rotate

STRUCTURE OF THE DSDNA BACTERIOPHAGE HK97 MATURE EMPTY CAPSID

Overview

The HK97 bacteriophage capsid is a unique example of macromolecular catenanes: interlocked rings of covalently attached protein subunits. The chain mail organization of the subunits stabilizes a particle in which the maximum thickness of the protein shell is 18A and the maximum diameter is 550A. The electron density has the appearance of a balloon illustrating the extraordinary strength conferred by the unique subunit organization. The refined structure shows novel qualities of the HK97 shell protein, gp5 that, together with the protease gp4, guides the assembly and maturation of the virion. Although gp5 forms hexamers and pentamers and the subunits exist in different structural environments, the tertiary structures of the seven protein molecules in the viral asymmetric unit are closely similar. The interactions of the subunits in the shell are exceptionally complex with each subunit interacting with nine other subunits. The interactions of the N-terminus released after gp5 cleavage appear important for organization of the loops that become crosslinked to the core of a neighboring subunit at the maturation. A comparison with a model of the Prohead II structure revealed that the surfaces of non-covalent contact between the monomers that build up hexamers/pentamers are completely redefined during maturation.

About this Structure

1OHG is a Single protein structure of sequence from Enterobacteria phage hk620 with and as ligands. This structure supersedes the now removed PDB entry 1FH6. The following page contains interesting information on the relation of 1OHG with [Citrate Synthase]. Full crystallographic information is available from OCA.

Reference

The refined structure of a protein catenane: the HK97 bacteriophage capsid at 3.44 A resolution., Helgstrand C, Wikoff WR, Duda RL, Hendrix RW, Johnson JE, Liljas L, J Mol Biol. 2003 Dec 12;334(5):885-99. PMID:14643655

Page seeded by OCA on Thu Feb 21 14:17:46 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools