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[[Image:2pro.gif|left|200px]]


{{Structure
==PRO REGION OF ALPHA-LYTIC PROTEASE==
|PDB= 2pro |SIZE=350|CAPTION= <scene name='initialview01'>2pro</scene>, resolution 3.0&Aring;
<StructureSection load='2pro' size='340' side='right'caption='[[2pro]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[2pro]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PRO FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2pro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pro OCA], [https://pdbe.org/2pro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pro RCSB], [https://www.ebi.ac.uk/pdbsum/2pro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pro ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pro OCA], [http://www.ebi.ac.uk/pdbsum/2pro PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pro RCSB]</span>
[https://www.uniprot.org/uniprot/PRLA_LYSEN PRLA_LYSEN]
}}
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pr/2pro_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pro ConSurf].
<div style="clear:both"></div>


'''PRO REGION OF ALPHA-LYTIC PROTEASE'''
==See Also==
 
*[[Alpha-lytic protease 3D structures|Alpha-lytic protease 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
2PRO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRO OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/9808037 9808037]
[[Category: Lysobacter enzymogenes]]
[[Category: Lysobacter enzymogenes]]
[[Category: Single protein]]
[[Category: Agard DA]]
[[Category: Agard, D A.]]
[[Category: Mau T]]
[[Category: Mau, T.]]
[[Category: Rader SD]]
[[Category: Rader, S D.]]
[[Category: Sauter NK]]
[[Category: Sauter, N K.]]
[[Category: foldase]]
[[Category: pro region]]
[[Category: protein folding]]
[[Category: serine protease]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:39:49 2008''

Latest revision as of 12:11, 21 February 2024

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

Structural highlights

2pro is a 3 chain structure with sequence from Lysobacter enzymogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PRLA_LYSEN

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2pro, resolution 3.00Å

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