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.


1mum

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1mum.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1mum.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1mum| PDB=1mum | SCENE= }}
{{STRUCTURE_1mum| PDB=1mum | SCENE= }}
-
'''Structure of the 2-Methylisocitrate Lyase (PrpB) from Escherichia coli'''
+
===Structure of the 2-Methylisocitrate Lyase (PrpB) from Escherichia coli===
-
==Overview==
+
<!--
-
Following acetate, propionate is the second most abundant low molecular mass carbon compound found in soil. Many microorganisms, including most, if not all fungi, as well as several aerobic bacteria, such as Escherichia coli and Salmonella enterica oxidize propionate via the methylcitrate cycle. The enzyme 2-methylisocitrate lyase (PrpB) from Escherichia coli catalysing the last step of this cycle, the cleavage of 2-methylisocitrate to pyruvate and succinate, was crystallised and its structure determined to a resolution of 1.9A. The enzyme, which strictly depends on Mg(2+) for catalysis, belongs to the isocitrate lyase protein family. A common feature of members of this enzyme family is the movement of a so-called "active site loop" from an open into a closed conformation upon substrate binding thus shielding the reactants from the surrounding solvent. Since in the presented structure, PrpB contains, apart from a Mg(2+), no ligand, the active site loop is found in an open conformation. This conformation, however, differs significantly from the open conformation present in the so far known structures of ligand-free isocitrate lyases. A possible impact of this observation with respect to the different responses of isocitrate lyases and PrpB upon treatment with the common inhibitor 3-bromopyruvate is discussed. Based on the structure of ligand-bound isocitrate lyase from Mycobacterium tuberculosis a model of the substrate-bound PrpB enzyme in its closed conformation was created which provides hints towards the substrate specificity of this enzyme.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12706720}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12706720 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12706720}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Prpb]]
[[Category: Prpb]]
[[Category: Tim-barrel]]
[[Category: Tim-barrel]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:44:20 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:12:51 2008''

Revision as of 13:12, 27 July 2008

Image:1mum.png

Template:STRUCTURE 1mum

Structure of the 2-Methylisocitrate Lyase (PrpB) from Escherichia coli

Template:ABSTRACT PUBMED 12706720

About this Structure

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

Reference

Crystal structure of 2-methylisocitrate lyase (PrpB) from Escherichia coli and modelling of its ligand bound active centre., Grimm C, Evers A, Brock M, Maerker C, Klebe G, Buckel W, Reuter K, J Mol Biol. 2003 May 2;328(3):609-21. PMID:12706720

Page seeded by OCA on Sun Jul 27 16:12:51 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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