This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1dp0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1dp0.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1dp0.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1dp0| PDB=1dp0 | SCENE= }}
{{STRUCTURE_1dp0| PDB=1dp0 | SCENE= }}
-
'''E. COLI BETA-GALACTOSIDASE AT 1.7 ANGSTROM'''
+
===E. COLI BETA-GALACTOSIDASE AT 1.7 ANGSTROM===
-
==Overview==
+
<!--
-
The unrefined fold of Escherichia coli beta-galactosidase based on a monoclinic crystal form with four independent tetramers has been reported previously. Here, we describe a new, orthorhombic form with one tetramer per asymmetric unit that has permitted refinement of the structure at 1.7 A resolution. This high-resolution analysis has confirmed the original description of the structure and revealed new details. An essential magnesium ion, identified at the active site in the monoclinic crystals, is also seen in the orthorhombic form. Additional putative magnesium binding sites are also seen. Sodium ions are also known to affect catalysis, and five putative binding sites have been identified, one close to the active site. In a crevice on the protein surface, five linked five-membered solvent rings form a partial clathrate-like structure. Some other unusual aspects of the structure include seven apparent cis-peptide bonds, four of which are proline, and several internal salt-bridge networks. Deep solvent-filled channels and tunnels extend across the surface of the molecule and pass through the center of the tetramer. Because of these departures from a compact globular shape, the molecule is not well characterized by prior empirical relationships between the mass and surface area of proteins. The 50 or so residues at the amino terminus have a largely extended conformation and mostly lie across the surface of the protein. At the same time, however, segment 13-21 contributes to a subunit interface, and residues 29-33 pass through a "tunnel" formed by a domain interface. Taken together, the overall arrangement provides a structural basis for the phenomenon of alpha-complementation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11045615}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11045615 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11045615}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Immunoglobulin]]
[[Category: Immunoglobulin]]
[[Category: Jelly-roll barrel]]
[[Category: Jelly-roll barrel]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:06:06 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:24:08 2008''

Revision as of 20:24, 30 June 2008

Image:1dp0.png

Template:STRUCTURE 1dp0

E. COLI BETA-GALACTOSIDASE AT 1.7 ANGSTROM

Template:ABSTRACT PUBMED 11045615

About this Structure

1DP0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

High resolution refinement of beta-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for alpha-complementation., Juers DH, Jacobson RH, Wigley D, Zhang XJ, Huber RE, Tronrud DE, Matthews BW, Protein Sci. 2000 Sep;9(9):1685-99. PMID:11045615

Page seeded by OCA on Mon Jun 30 23:24:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dp0"
Personal tools