2pro: Difference between revisions

Revision as of 21:00, 28 July 2008

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File:2pro.png

Template:STRUCTURE 2pro

PRO REGION OF ALPHA-LYTIC PROTEASEPRO REGION OF ALPHA-LYTIC PROTEASE

Template:ABSTRACT PUBMED 9808037

About this StructureAbout this Structure

2PRO is a Single protein structure of sequence from Lysobacter enzymogenes. Full crystallographic information is available from OCA.

ReferenceReference

Structure of alpha-lytic protease complexed with its pro region., Sauter NK, Mau T, Rader SD, Agard DA, Nat Struct Biol. 1998 Nov;5(11):945-50. PMID:9808037

Page seeded by OCA on Mon Jul 28 21:00:20 2008

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OCA

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-[[Image:2pro.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_2pro|  PDB=2pro  |  SCENE=  }}
-'''PRO REGION OF ALPHA-LYTIC PROTEASE'''
+===PRO REGION OF ALPHA-LYTIC PROTEASE===
-==Overview==
+<!--
-While the majority of proteins fold rapidly and spontaneously to their native states, the extracellular bacterial protease alpha-lytic protease (alphaLP) has a t(1/2) for folding of approximately 2,000 years, corresponding to a folding barrier of 30 kcal mol(-1). AlphaLP is synthesized as a pro-enzyme where its pro region (Pro) acts as a foldase to stabilize the transition state for the folding reaction. Pro also functions as a potent folding catalyst when supplied as a separate polypeptide chain, accelerating the rate of alphaLP folding by a factor of 3 x 10(9). In the absence of Pro, alphaLP folds only partially to a stable molten globule-like intermediate state. Addition of Pro to this intermediate leads to rapid formation of native alphaLP. Here we report the crystal structures of Pro and of the non-covalent inhibitory complex between Pro and native alphaLP. The C-shaped Pro surrounds the C-terminal beta-barrel domain of the folded protease, forming a large complementary interface. Regions of extensive hydration in the interface explain how Pro binds tightly to the native state, yet even more tightly to the folding transition state. Based on structural and functional data we propose that a specific structural element in alphaLP is largely responsible for the folding barrier and suggest how Pro can overcome this barrier.
+The line below this paragraph, {{ABSTRACT_PUBMED_9808037}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9808037 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9808037}}
 ==About this Structure==
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 [[Category: Protein folding]]
 [[Category: Serine protease]]
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