2h5c

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[[Image:2h5c.gif|left|200px]]<br /><applet load="2h5c" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2h5c.gif|left|200px]]
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caption="2h5c, resolution 0.82&Aring;" />
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'''0.82A resolution crystal structure of alpha-lytic protease at pH 5'''<br />
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{{Structure
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|PDB= 2h5c |SIZE=350|CAPTION= <scene name='initialview01'>2h5c</scene>, resolution 0.82&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12]
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|GENE=
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}}
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'''0.82A resolution crystal structure of alpha-lytic protease at pH 5'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2H5C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H5C OCA].
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2H5C 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=2H5C OCA].
==Reference==
==Reference==
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Subangstrom crystallography reveals that short ionic hydrogen bonds, and not a His-Asp low-barrier hydrogen bond, stabilize the transition state in serine protease catalysis., Fuhrmann CN, Daugherty MD, Agard DA, J Am Chem Soc. 2006 Jul 19;128(28):9086-102. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16834383 16834383]
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Subangstrom crystallography reveals that short ionic hydrogen bonds, and not a His-Asp low-barrier hydrogen bond, stabilize the transition state in serine protease catalysis., Fuhrmann CN, Daugherty MD, Agard DA, J Am Chem Soc. 2006 Jul 19;128(28):9086-102. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16834383 16834383]
[[Category: Alpha-lytic endopeptidase]]
[[Category: Alpha-lytic endopeptidase]]
[[Category: Lysobacter enzymogenes]]
[[Category: Lysobacter enzymogenes]]
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[[Category: ultra-high resolution]]
[[Category: ultra-high resolution]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:38:29 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:12:54 2008''

Revision as of 15:12, 20 March 2008

Image:2h5c.gif


PDB ID 2h5c

Drag the structure with the mouse to rotate
, resolution 0.82Å
Ligands: and
Activity: Alpha-lytic endopeptidase, with EC number 3.4.21.12
Coordinates: save as pdb, mmCIF, xml



0.82A resolution crystal structure of alpha-lytic protease at pH 5


Overview

To address questions regarding the mechanism of serine protease catalysis, we have solved two X-ray crystal structures of alpha-lytic protease (alphaLP) that mimic aspects of the transition states: alphaLP at pH 5 (0.82 A resolution) and alphaLP bound to the peptidyl boronic acid inhibitor, MeOSuc-Ala-Ala-Pro-boroVal (0.90 A resolution). Based on these structures, there is no evidence of, or requirement for, histidine-flipping during the acylation step of the reaction. Rather, our data suggests that upon protonation of His57, Ser195 undergoes a conformational change that destabilizes the His57-Ser195 hydrogen bond, preventing the back-reaction. In both structures the His57-Asp102 hydrogen bond in the catalytic triad is a normal ionic hydrogen bond, and not a low-barrier hydrogen bond (LBHB) as previously hypothesized. We propose that the enzyme has evolved a network of relatively short hydrogen bonds that collectively stabilize the transition states. In particular, a short ionic hydrogen bond (SIHB) between His57 Nepsilon2 and the substrate's leaving group may promote forward progression of the TI1-to-acylenzyme reaction. We provide experimental evidence that refutes use of either a short donor-acceptor distance or a downfield 1H chemical shift as sole indicators of a LBHB.

About this Structure

2H5C is a Single protein structure of sequence from Lysobacter enzymogenes. Full crystallographic information is available from OCA.

Reference

Subangstrom crystallography reveals that short ionic hydrogen bonds, and not a His-Asp low-barrier hydrogen bond, stabilize the transition state in serine protease catalysis., Fuhrmann CN, Daugherty MD, Agard DA, J Am Chem Soc. 2006 Jul 19;128(28):9086-102. PMID:16834383

Page seeded by OCA on Thu Mar 20 17:12:54 2008

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