1i1i
From Proteopedia
(New page: 200px<br /><applet load="1i1i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i1i, resolution 2.3Å" /> '''NEUROLYSIN (ENDOPEPTI...) |
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| - | [[Image:1i1i.gif|left|200px]]<br /><applet load="1i1i" size=" | + | [[Image:1i1i.gif|left|200px]]<br /><applet load="1i1i" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1i1i, resolution 2.3Å" /> | caption="1i1i, resolution 2.3Å" /> | ||
'''NEUROLYSIN (ENDOPEPTIDASE 24.16) CRYSTAL STRUCTURE'''<br /> | '''NEUROLYSIN (ENDOPEPTIDASE 24.16) CRYSTAL STRUCTURE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The zinc metallopeptidase neurolysin is shown by x-ray crystallography to | + | The zinc metallopeptidase neurolysin is shown by x-ray crystallography to have large structural elements erected over the active site region that allow substrate access only through a deep narrow channel. This architecture accounts for specialization of this neuropeptidase to small bioactive peptide substrates without bulky secondary and tertiary structures. In addition, modeling studies indicate that the length of a substrate N-terminal to the site of hydrolysis is restricted to approximately 10 residues by the limited size of the active site cavity. Some structural elements of neurolysin, including a five-stranded beta-sheet and the two active site helices, are conserved with other metallopeptidases. The connecting loop regions of these elements, however, are much extended in neurolysin, and they, together with other open coil elements, line the active site cavity. These potentially flexible elements may account for the ability of the enzyme to cleave a variety of sequences. |
==About this Structure== | ==About this Structure== | ||
| - | 1I1I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Neurolysin Neurolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.16 3.4.24.16] Full crystallographic information is available from [http:// | + | 1I1I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Neurolysin Neurolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.16 3.4.24.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1I OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Beck, M | + | [[Category: Beck, M R.]] |
| - | [[Category: Brown, C | + | [[Category: Brown, C K.]] |
[[Category: Lian, W.]] | [[Category: Lian, W.]] | ||
[[Category: Madauss, K.]] | [[Category: Madauss, K.]] | ||
| - | [[Category: Rodgers, D | + | [[Category: Rodgers, D W.]] |
| - | [[Category: Tolbert, W | + | [[Category: Tolbert, W D.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: endopeptidase]] | [[Category: endopeptidase]] | ||
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[[Category: zinc metallopeptidase]] | [[Category: zinc metallopeptidase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:06:59 2008'' |
Revision as of 11:07, 21 February 2008
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NEUROLYSIN (ENDOPEPTIDASE 24.16) CRYSTAL STRUCTURE
Overview
The zinc metallopeptidase neurolysin is shown by x-ray crystallography to have large structural elements erected over the active site region that allow substrate access only through a deep narrow channel. This architecture accounts for specialization of this neuropeptidase to small bioactive peptide substrates without bulky secondary and tertiary structures. In addition, modeling studies indicate that the length of a substrate N-terminal to the site of hydrolysis is restricted to approximately 10 residues by the limited size of the active site cavity. Some structural elements of neurolysin, including a five-stranded beta-sheet and the two active site helices, are conserved with other metallopeptidases. The connecting loop regions of these elements, however, are much extended in neurolysin, and they, together with other open coil elements, line the active site cavity. These potentially flexible elements may account for the ability of the enzyme to cleave a variety of sequences.
About this Structure
1I1I is a Single protein structure of sequence from Rattus norvegicus with as ligand. Active as Neurolysin, with EC number 3.4.24.16 Full crystallographic information is available from OCA.
Reference
Structure of neurolysin reveals a deep channel that limits substrate access., Brown CK, Madauss K, Lian W, Beck MR, Tolbert WD, Rodgers DW, Proc Natl Acad Sci U S A. 2001 Mar 13;98(6):3127-32. Epub 2001 Mar 6. PMID:11248043
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