2pro: Difference between revisions

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<StructureSection load='2pro' size='340' side='right'caption='[[2pro]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='2pro' size='340' side='right'caption='[[2pro]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2pro]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_29487 Atcc 29487]. 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>
<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>
</td></tr><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>
</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>
<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>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRLA_LYSEN PRLA_LYSEN]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:9808037</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2pro" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Alpha-lytic protease 3D structures|Alpha-lytic protease 3D structures]]
*[[Alpha-lytic protease 3D structures|Alpha-lytic protease 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 29487]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Agard, D A]]
[[Category: Lysobacter enzymogenes]]
[[Category: Mau, T]]
[[Category: Agard DA]]
[[Category: Rader, S D]]
[[Category: Mau T]]
[[Category: Sauter, N K]]
[[Category: Rader SD]]
[[Category: Foldase]]
[[Category: Sauter NK]]
[[Category: Pro region]]
[[Category: Protein folding]]
[[Category: Serine protease]]

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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