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2iy1

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(New page: 200px<br /> <applet load="2iy1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iy1, resolution 2.46&Aring;" /> '''SENP1 (MUTANT) FULL...)
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'''SENP1 (MUTANT) FULL LENGTH SUMO1'''<br />
'''SENP1 (MUTANT) FULL LENGTH SUMO1'''<br />
==Overview==
==Overview==
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Small ubiquitin-like modifier (SUMO)-specific protease SENP1 processes, SUMO-1, SUMO-2 and SUMO-3 to mature forms and deconjugates them from, modified proteins. To establish the proteolytic mechanism, we determined, structures of catalytically inactive SENP1 bound to SUMO-1-modified, RanGAP1 and to unprocessed SUMO-1. In each case, the scissile peptide bond, is kinked at a right angle to the C-terminal tail of SUMO-1 and has the, cis configuration of the amide nitrogens. SENP1 preferentially processes, SUMO-1 over SUMO-2, but binding thermodynamics of full-length SUMO-1 and, SUMO-2 to SENP1 and K(m) values for processing are very similar. However, k(cat) values differ by 50-fold. Thus, discrimination between unprocessed, SUMO-1 and SUMO-2 by SENP1 is based on a catalytic step rather than, substrate binding and is likely to reflect differences in the ability of, SENP1 to correctly orientate the scissile bonds in SUMO-1 and SUMO-2.
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Small ubiquitin-like modifier (SUMO)-specific protease SENP1 processes SUMO-1, SUMO-2 and SUMO-3 to mature forms and deconjugates them from modified proteins. To establish the proteolytic mechanism, we determined structures of catalytically inactive SENP1 bound to SUMO-1-modified RanGAP1 and to unprocessed SUMO-1. In each case, the scissile peptide bond is kinked at a right angle to the C-terminal tail of SUMO-1 and has the cis configuration of the amide nitrogens. SENP1 preferentially processes SUMO-1 over SUMO-2, but binding thermodynamics of full-length SUMO-1 and SUMO-2 to SENP1 and K(m) values for processing are very similar. However, k(cat) values differ by 50-fold. Thus, discrimination between unprocessed SUMO-1 and SUMO-2 by SENP1 is based on a catalytic step rather than substrate binding and is likely to reflect differences in the ability of SENP1 to correctly orientate the scissile bonds in SUMO-1 and SUMO-2.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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2IY1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IY1 OCA].
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2IY1 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IY1 OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Dong, C.]]
[[Category: Dong, C.]]
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[[Category: Naismith, J.H.]]
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[[Category: Naismith, J H.]]
[[Category: Shen, L.]]
[[Category: Shen, L.]]
[[Category: hydrolase]]
[[Category: hydrolase]]
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[[Category: ubl conjugation pathway]]
[[Category: ubl conjugation pathway]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:49:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:57:13 2008''

Revision as of 15:57, 21 February 2008

Image:2iy1.gif

2iy1, resolution 2.46Å

Drag the structure with the mouse to rotate

SENP1 (MUTANT) FULL LENGTH SUMO1

Contents

Overview

Small ubiquitin-like modifier (SUMO)-specific protease SENP1 processes SUMO-1, SUMO-2 and SUMO-3 to mature forms and deconjugates them from modified proteins. To establish the proteolytic mechanism, we determined structures of catalytically inactive SENP1 bound to SUMO-1-modified RanGAP1 and to unprocessed SUMO-1. In each case, the scissile peptide bond is kinked at a right angle to the C-terminal tail of SUMO-1 and has the cis configuration of the amide nitrogens. SENP1 preferentially processes SUMO-1 over SUMO-2, but binding thermodynamics of full-length SUMO-1 and SUMO-2 to SENP1 and K(m) values for processing are very similar. However, k(cat) values differ by 50-fold. Thus, discrimination between unprocessed SUMO-1 and SUMO-2 by SENP1 is based on a catalytic step rather than substrate binding and is likely to reflect differences in the ability of SENP1 to correctly orientate the scissile bonds in SUMO-1 and SUMO-2.

Disease

Known diseases associated with this structure: Orofacial cleft 10 OMIM:[601912]

About this Structure

2IY1 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

SUMO protease SENP1 induces isomerization of the scissile peptide bond., Shen L, Tatham MH, Dong C, Zagorska A, Naismith JH, Hay RT, Nat Struct Mol Biol. 2006 Dec;13(12):1069-77. Epub 2006 Nov 12. PMID:17099698

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