1mat

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[[Image:1mat.jpg|left|200px]]
[[Image:1mat.jpg|left|200px]]
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{{Structure
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|PDB= 1mat |SIZE=350|CAPTION= <scene name='initialview01'>1mat</scene>, resolution 2.4&Aring;
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The line below this paragraph, containing "STRUCTURE_1mat", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </span>
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|GENE=
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{{STRUCTURE_1mat| PDB=1mat | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mat OCA], [http://www.ebi.ac.uk/pdbsum/1mat PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mat RCSB]</span>
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}}
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'''STRUCTURE OF THE COBALT-DEPENDENT METHIONINE AMINOPEPTIDASE FROM ESCHERICHIA COLI: A NEW TYPE OF PROTEOLYTIC ENZYME'''
'''STRUCTURE OF THE COBALT-DEPENDENT METHIONINE AMINOPEPTIDASE FROM ESCHERICHIA COLI: A NEW TYPE OF PROTEOLYTIC ENZYME'''
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[[Category: Matthews, B W.]]
[[Category: Matthews, B W.]]
[[Category: Roderick, S L.]]
[[Category: Roderick, S L.]]
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[[Category: hydrolase(alpha-aminoacylpeptide)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:50:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:13:41 2008''
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Revision as of 21:50, 2 May 2008

Image:1mat.jpg

Template:STRUCTURE 1mat

STRUCTURE OF THE COBALT-DEPENDENT METHIONINE AMINOPEPTIDASE FROM ESCHERICHIA COLI: A NEW TYPE OF PROTEOLYTIC ENZYME


Overview

The X-ray structure of Escherichia coli methionine aminopeptidase (MAP) has been determined to 2.4-A resolution and refined to a crystallographic R-factor of 18.2%. The fold is novel and displays internal pseudo-2-fold symmetry which structurally relates the first and second halves of the polypeptide chain. The topology consists of a central antiparallel beta-sheet covered on one side by two pairs of alpha-helices and by a C-terminal loop. The other face of the beta-sheet, together with some irregular loops, forms the active site, which contains two cobalt ions 2.9 A apart. These metal ions are liganded by the side chains of Asp 97, Asp 108, Glu 204, Glu 235, and His 171 with approximate octahedral coordination. In terms of both the novel backbone fold and the constitution of the active site, MAP appears to represent a new class of proteolytic enzyme.

About this Structure

1MAT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme., Roderick SL, Matthews BW, Biochemistry. 1993 Apr 20;32(15):3907-12. PMID:8471602 Page seeded by OCA on Sat May 3 00:50:10 2008

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