2f91: Difference between revisions

Revision as of 16:10, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2f91.png

Template:STRUCTURE 2f91

1.2A resolution structure of a crayfish trypsin complexed with a peptide inhibitor, SGTI1.2A resolution structure of a crayfish trypsin complexed with a peptide inhibitor, SGTI

Template:ABSTRACT PUBMED 16475800

About this StructureAbout this Structure

2F91 is a Protein complex structure of sequences from Pontastacus leptodactylus. This structure supersedes the now removed PDB entry 1yr4. Full crystallographic information is available from OCA.

ReferenceReference

Enzyme:substrate hydrogen bond shortening during the acylation phase of serine protease catalysis., Fodor K, Harmat V, Neutze R, Szilagyi L, Graf L, Katona G, Biochemistry. 2006 Feb 21;45(7):2114-21. PMID:16475800

Extended intermolecular interactions in a serine protease-canonical inhibitor complex account for strong and highly specific inhibition., Fodor K, Harmat V, Hetenyi C, Kardos J, Antal J, Perczel A, Patthy A, Katona G, Graf L, J Mol Biol. 2005 Jul 1;350(1):156-69. PMID:15922357

Page seeded by OCA on Mon Jul 28 16:10:26 2008

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

OCA

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-[[Image:2f91.gif|left|200px]]
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 {{STRUCTURE_2f91|  PDB=2f91  |  SCENE=  }}
-'''1.2A resolution structure of a crayfish trypsin complexed with a peptide inhibitor, SGTI'''
+===1.2A resolution structure of a crayfish trypsin complexed with a peptide inhibitor, SGTI===
-==Overview==
+<!--
-Atomic resolution (&lt;or=1.2 A) serine protease intermediate structures revealed that the strength of the hydrogen bonds between the enzyme and the substrate changed during catalysis. The well-conserved hydrogen bonds of antiparallel beta-sheet between the enzyme and the substrate become significantly shorter in the transition from a Michaelis complex analogue (Pontastacus leptodactylus (narrow-fingered crayfish) trypsin (CFT) in complex with Schistocerca gregaria (desert locust) trypsin inhibitor (SGTI) at 1.2 A resolution) to an acyl-enzyme intermediate (N-acetyl-Asn-Pro-Ile acyl-enzyme intermediate of porcine pancreatic elastase at 0.95 A resolution) presumably synchronously with the nucleophilic attack on the carbonyl carbon atom of the scissile peptide bond. This is interpreted as an active mechanism that utilizes the energy released from the stronger hydrogen bonds to overcome the energetic barrier of the nucleophilic attack by the hydroxyl group of the catalytic serine. In the CFT:SGTI complex this hydrogen bond shortening may be hindered by the 27I-32I disulfide bridge and Asn-15I of SGTI. The position of the catalytic histidine changes slightly as it adapts to the different nucleophilic attacker during the transition from the Michaelis complex to the acyl-enzyme state, and simultaneously its interaction with Asp-102 and Ser-214 becomes stronger. The oxyanion hole hydrogen bonds provide additional stabilization for acyl-ester bond in the acyl-enzyme than for scissile peptide bond of the Michaelis complex. Significant deviation from planarity is not observed in the reactive bonds of either the Michaelis complex or the acyl-enzyme. In the Michaelis complex the electron distribution of the carbonyl bond is distorted toward the oxygen atom compared to other peptide bonds in the structure, which indicates the polarization effect of the oxyanion hole.
+The line below this paragraph, {{ABSTRACT_PUBMED_16475800}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16475800 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16475800}}
 ==About this Structure==
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 ==Reference==
 Enzyme:substrate hydrogen bond shortening during the acylation phase of serine protease catalysis., Fodor K, Harmat V, Neutze R, Szilagyi L, Graf L, Katona G, Biochemistry. 2006 Feb 21;45(7):2114-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16475800 16475800]
+Extended intermolecular interactions in a serine protease-canonical inhibitor complex account for strong and highly specific inhibition., Fodor K, Harmat V, Hetenyi C, Kardos J, Antal J, Perczel A, Patthy A, Katona G, Graf L, J Mol Biol. 2005 Jul 1;350(1):156-69. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15922357 15922357]
 [[Category: Pontastacus leptodactylus]]
 [[Category: Protein complex]]
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 [[Category: Serine protease]]
 [[Category: Trypsin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 03:36:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:10:26 2008''